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Conserved domains on  [gi|1733579917|dbj|GCA70988|]
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phycocyanobilin lyase subunit alpha [Microcystis aeruginosa NIES-2519]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HEAT COG1413
HEAT repeat [General function prediction only];
210-346 2.84e-42

HEAT repeat [General function prediction only];


:

Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 149.78  E-value: 2.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 210 VRRNAAFALGNIGSETAIQELLKALEDsDDWSVRRNAAFALAEIGTETAIPELLKALEDSNKDVRIKAAEALGKIGSETA 289
Cdd:COG1413     1 VRRAAARALGRLGDPAAVPALIAALAD-EDPDVRAAAARALGRLGDPRAVPALLEALKDPDPEVRAAAAEALGRIGDPEA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1733579917 290 ITGLLKALKDSNSIVRIKAAKALGNIGSETVIPGLLKALEDSDRYVRRDAAQALGKI 346
Cdd:COG1413    80 VPALIAALKDEDPEVRRAAAEALGRLGDPAAVPALLEALKDPDWEVRRAAARALGRL 136
HEAT COG1413
HEAT repeat [General function prediction only];
24-159 9.73e-41

HEAT repeat [General function prediction only];


:

Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 145.54  E-value: 9.73e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  24 VRGYAAFALGKIGSETAIGGLLKALEDSDEYVRRSAAFALGKIGSETAIGGLLKALEDSDEYVRMYAAKALGNIGSETAI 103
Cdd:COG1413     1 VRRAAARALGRLGDPAAVPALIAALADEDPDVRAAAARALGRLGDPRAVPALLEALKDPDPEVRAAAAEALGRIGDPEAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1733579917 104 TGLLKALEDSDEDVLWNAAEALGKIGTETTIAGLLKALEDSNKDVREYAAYALGNI 159
Cdd:COG1413    81 PALIAALKDEDPEVRRAAAEALGRLGDPAAVPALLEALKDPDWEVRRAAARALGRL 136
HEAT COG1413
HEAT repeat [General function prediction only];
304-440 1.71e-40

HEAT repeat [General function prediction only];


:

Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 144.77  E-value: 1.71e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 304 VRIKAAKALGNIGSETVIPGLLKALEDSDRYVRRDAAQALGKISSETAIAGLLKALKDSYFSVRWKAVEALGKIGSETAI 383
Cdd:COG1413     1 VRRAAARALGRLGDPAAVPALIAALADEDPDVRAAAARALGRLGDPRAVPALLEALKDPDPEVRAAAAEALGRIGDPEAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1733579917 384 PGLLKALEDSNSILRWKAAEALGNIGSETAIPGLLKALEHSNSNVRVYAAVALGKIG 440
Cdd:COG1413    81 PALIAALKDEDPEVRRAAAEALGRLGDPAAVPALLEALKDPDWEVRRAAARALGRLG 137
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 165-251 2.96e-19

HEAT repeats; This family includes multiple HEAT repeats.


:

Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 82.77  E-value: 2.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 165 IAGLLKAL-EHSNSDVRGYAAFALGKIGSETAIGGLLKALEDSDEYVRRNAAFALGNIGSETAIQELLKALEDSDDWSVR 243
Cdd:pfam13646   1 LPALLQALlRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDEDPAVRRAAAEALGKIGDPEALPALLELLRDDDDDVVR 80


                  ....*...
gi 1733579917 244 RNAAFALA 251
Cdd:pfam13646  81 AAAAEALA 88
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
 494-606 2.89e-13

TIR domain; This is a family of Toll-like receptors.


:

Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 66.57  E-value: 2.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 494 VYISYNWqEDSnEMANQLVQAFDAKGIEIIRDKTHTSYKDSIKNFMRQ-IGRGKCVVAVISDRYLKSENCMFELVEIARN 572
Cdd:pfam13676   1 VFISYAG-EDR-AWAEWLADALEAAGYRVWLDRWDIRPGDDWVEEIEEaIENSDRVLVVLSPNYLESPWCRAEWEAALAD 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1733579917 573 GDFYKRIFPIILPDARIYKDFERIDYLKYWEDEK 606
Cdd:pfam13676  79 PEGRKRLIPVRLECDLELPGLAGLQYIDLRDGDE 112
QueG super family cl34317
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 1-38 6.01e-03

Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; Epoxyqueuosine reductase QueG (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


The actual alignment was detected with superfamily member COG1600:

Pssm-ID: 441208 [Multi-domain]  Cd Length: 345  Bit Score: 39.42  E-value: 6.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1733579917   1 MGNISSETAIAGLLKALEHSNSDVRGYAAFALGKIGSE 38
Cdd:COG1600   307 LGNSGDPAAVPALEALLDDPSPLVREHAAWALGRLGGR 344
HEAT_PBS pfam03130
PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to ...
 428-454 8.78e-03

PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to pfam02985. Cyanobacteria and red algae harvest light energy using macromolecular complexes known as phycobilisomes (PBS), peripherally attached to the photosynthetic membrane. The major components of PBS are the phycobiliproteins. These heterodimeric proteins are covalently attached to phycobilins: open-chain tetrapyrrole chromophores, which function as the photosynthetic light-harvesting pigments. Phycobiliproteins differ in sequence and in the nature and number of attached phycobilins to each of their subunits. This family includes the lyase enzymes that specifically attach particular phycobilins to apophycobiliprotein subunits. The most comprehensively studied of these is the CpcE/F lyase, which attaches phycocyanobilin (PCB) to the alpha subunit of apophycocyanin. Similarly, MpeU/V attaches phycoerythrobilin to phycoerythrin II, while CpeY/Z is thought to be involved in phycoerythrobilin (PEB) attachment to phycoerythrin (PE) I (PEs I and II differ in sequence and in the number of attached molecules of PEB: PE I has five, PE II has six). All the reactions of the above lyases involve an apoprotein cysteine SH addition to a terminal delta 3,3'-double bond. Such a reaction is not possible in the case of phycoviolobilin (PVB), the phycobilin of alpha-phycoerythrocyanin (alpha-PEC). It is thought that in this case, PCB, not PVB, is first added to apo-alpha-PEC, and is then isomerized to PVB. The addition reaction has been shown to occur in the presence of either of the components of alpha-PEC-PVB lyase PecE or PecF (or both). The isomerization reaction occurs only when both PecE and PecF components are present, i.e. the PecE/F phycobiliprotein lyase is also a phycobilin isomerase. Another member of this family is the NblB protein, whose similarity to the phycobiliprotein lyases was previously noted. This constitutively expressed protein is not known to have any lyase activity. It is thought to be involved in the coordination of PBS degradation with environmental nutrient limitation. It has been suggested that the similarity of NblB to the phycobiliprotein lyases is due to the ability to bind tetrapyrrole phycobilins via the common repeated motif.


:

Pssm-ID: 308641 [Multi-domain]  Cd Length: 27  Bit Score: 34.38  E-value: 8.78e-03
                          10        20
                  ....*....|....*....|....*..
gi 1733579917 428 VRVYAAVALGKIGTEAAMTELIKCLKN 454
Cdd:pfam03130   1 VRRAAARALGALGDPEAIPALIEALDD 27
 
Name Accession Description Interval E-value
HEAT COG1413
HEAT repeat [General function prediction only];
210-346 2.84e-42

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 149.78  E-value: 2.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 210 VRRNAAFALGNIGSETAIQELLKALEDsDDWSVRRNAAFALAEIGTETAIPELLKALEDSNKDVRIKAAEALGKIGSETA 289
Cdd:COG1413     1 VRRAAARALGRLGDPAAVPALIAALAD-EDPDVRAAAARALGRLGDPRAVPALLEALKDPDPEVRAAAAEALGRIGDPEA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1733579917 290 ITGLLKALKDSNSIVRIKAAKALGNIGSETVIPGLLKALEDSDRYVRRDAAQALGKI 346
Cdd:COG1413    80 VPALIAALKDEDPEVRRAAAEALGRLGDPAAVPALLEALKDPDWEVRRAAARALGRL 136
HEAT COG1413
HEAT repeat [General function prediction only];
24-159 9.73e-41

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 145.54  E-value: 9.73e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  24 VRGYAAFALGKIGSETAIGGLLKALEDSDEYVRRSAAFALGKIGSETAIGGLLKALEDSDEYVRMYAAKALGNIGSETAI 103
Cdd:COG1413     1 VRRAAARALGRLGDPAAVPALIAALADEDPDVRAAAARALGRLGDPRAVPALLEALKDPDPEVRAAAAEALGRIGDPEAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1733579917 104 TGLLKALEDSDEDVLWNAAEALGKIGTETTIAGLLKALEDSNKDVREYAAYALGNI 159
Cdd:COG1413    81 PALIAALKDEDPEVRRAAAEALGRLGDPAAVPALLEALKDPDWEVRRAAARALGRL 136
HEAT COG1413
HEAT repeat [General function prediction only];
304-440 1.71e-40

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 144.77  E-value: 1.71e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 304 VRIKAAKALGNIGSETVIPGLLKALEDSDRYVRRDAAQALGKISSETAIAGLLKALKDSYFSVRWKAVEALGKIGSETAI 383
Cdd:COG1413     1 VRRAAARALGRLGDPAAVPALIAALADEDPDVRAAAARALGRLGDPRAVPALLEALKDPDPEVRAAAAEALGRIGDPEAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1733579917 384 PGLLKALEDSNSILRWKAAEALGNIGSETAIPGLLKALEHSNSNVRVYAAVALGKIG 440
Cdd:COG1413    81 PALIAALKDEDPEVRRAAAEALGRLGDPAAVPALLEALKDPDWEVRRAAARALGRLG 137
PRK13800 PRK13800
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
162-436 1.09e-22

fumarate reductase/succinate dehydrogenase flavoprotein subunit;


Pssm-ID: 237512 [Multi-domain]  Cd Length: 897  Bit Score: 103.78  E-value: 1.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 162 ETAIAGLLKALEHSNSDVRGYAAFALGKIGSETAIGGLLKALEDSDEYVRRNAAFALGNI----GSETAIQELLkaleDS 237
Cdd:PRK13800  620 APSVAELAPYLADPDPGVRRTAVAVLTETTPPGFGPALVAALGDGAAAVRRAAAEGLRELvevlPPAPALRDHL----GS 695

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 238 DDWSVRRNAAFALAEIGTETAIpELLKALEDSNKDVRIKAAEALGkigSETAITGLLKALKDSNSIVRIKAAKALGNIGS 317
Cdd:PRK13800  696 PDPVVRAAALDVLRALRAGDAA-LFAAALGDPDHRVRIEAVRALV---SVDDVESVAGAATDENREVRIAVAKGLATLGA 771

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 318 ETVIPG-LLKAL-EDSDRYVRRDAAQALGKISSETAIAG-LLKALKDSYFSVRWKAVEALGKIGSETAIPGLLKALEDSN 394
Cdd:PRK13800  772 GGAPAGdAVRALtGDPDPLVRAAALAALAELGCPPDDVAaATAALRASAWQVRQGAARALAGAAADVAVPALVEALTDPH 851

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1733579917 395 SILRWKAAEALGNI-GSETAIPGLLKALEHSNSNVRVYAAVAL 436
Cdd:PRK13800  852 LDVRKAAVLALTRWpGDPAARDALTTALTDSDADVRAYARRAL 894
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 227-313 3.27e-21

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 88.55  E-value: 3.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 227 IQELLKALEDSDDWSVRRNAAFALAEIGTETAIPELLKALEDSNKDVRIKAAEALGKIGSETAITGLLKALK-DSNSIVR 305
Cdd:pfam13646   1 LPALLQALLRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDEDPAVRRAAAEALGKIGDPEALPALLELLRdDDDDVVR 80


                  ....*...
gi 1733579917 306 IKAAKALG 313
Cdd:pfam13646  81 AAAAEALA 88
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 165-251 2.96e-19

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 82.77  E-value: 2.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 165 IAGLLKAL-EHSNSDVRGYAAFALGKIGSETAIGGLLKALEDSDEYVRRNAAFALGNIGSETAIQELLKALEDSDDWSVR 243
Cdd:pfam13646   1 LPALLQALlRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDEDPAVRRAAAEALGKIGDPEALPALLELLRDDDDDVVR 80


                  ....*...
gi 1733579917 244 RNAAFALA 251
Cdd:pfam13646  81 AAAAEALA 88
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 321-406 9.74e-18

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 78.53  E-value: 9.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 321 IPGLLKAL-EDSDRYVRRDAAQALGKISSETAIAGLLKALKDSYFSVRWKAVEALGKIGSETAIPGLLKAL-EDSNSILR 398
Cdd:pfam13646   1 LPALLQALlRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDEDPAVRRAAAEALGKIGDPEALPALLELLrDDDDDVVR 80


                  ....*...
gi 1733579917 399 WKAAEALG 406
Cdd:pfam13646  81 AAAAEALA 88
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 44-126 4.07e-17

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 76.61  E-value: 4.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  44 LLKAL-EDSDEYVRRSAAFALGKIGSETAIGGLLKALEDSDEYVRMYAAKALGNIGSETAITGLLKAL-EDSDEDVLWNA 121
Cdd:pfam13646   4 LLQALlRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDEDPAVRRAAAEALGKIGDPEALPALLELLrDDDDDVVRAAA 83


                  ....*
gi 1733579917 122 AEALG 126
Cdd:pfam13646  84 AEALA 88
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
 494-606 2.89e-13

TIR domain; This is a family of Toll-like receptors.


Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 66.57  E-value: 2.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 494 VYISYNWqEDSnEMANQLVQAFDAKGIEIIRDKTHTSYKDSIKNFMRQ-IGRGKCVVAVISDRYLKSENCMFELVEIARN 572
Cdd:pfam13676   1 VFISYAG-EDR-AWAEWLADALEAAGYRVWLDRWDIRPGDDWVEEIEEaIENSDRVLVVLSPNYLESPWCRAEWEAALAD 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1733579917 573 GDFYKRIFPIILPDARIYKDFERIDYLKYWEDEK 606
Cdd:pfam13676  79 PEGRKRLIPVRLECDLELPGLAGLQYIDLRDGDE 112
PRK13800 PRK13800
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
11-251 5.94e-13

fumarate reductase/succinate dehydrogenase flavoprotein subunit;


Pssm-ID: 237512 [Multi-domain]  Cd Length: 897  Bit Score: 72.58  E-value: 5.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  11 AGLLKALEHSNSDVRGYAAFALGKI----GSETAIGGLLkaleDSDEYVRRSAAFALGKIGSETAIGGLLKALEDSDEYV 86
Cdd:PRK13800  655 PALVAALGDGAAAVRRAAAEGLRELvevlPPAPALRDHL----GSPDPVVRAAALDVLRALRAGDAALFAAALGDPDHRV 730

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  87 RMYAAKALGNIGSETAITGllkALEDSDEDVLWNAAEALGKIGTET-TIAGLLKAL-EDSNKDVREYAAYALGNISSETA 164
Cdd:PRK13800  731 RIEAVRALVSVDDVESVAG---AATDENREVRIAVAKGLATLGAGGaPAGDAVRALtGDPDPLVRAAALAALAELGCPPD 807

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 165 IAG-LLKALEHSNSDVRGYAAFALGKIGSETAIGGLLKALEDSDEYVRRNAAFALGNI-GSETAIQELLKALEDSDDwSV 242
Cdd:PRK13800  808 DVAaATAALRASAWQVRQGAARALAGAAADVAVPALVEALTDPHLDVRKAAVLALTRWpGDPAARDALTTALTDSDA-DV 886


                  ....*....
gi 1733579917 243 RRNAAFALA 251
Cdd:PRK13800  887 RAYARRALA 895
PDS5 cd19953
Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. ...
 258-377 8.40e-09

Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. Together with WapI and Scc3, it is involved in the release of the cohesin complex from chromosomes during S phase. The core of the cohesin complex consists of a coiled-coiled heterodimer of Smc1 and Smc30, together with Scc1 (also called kleisin). Pds5 interacts with Scc1 via a conserved patch on the surface of its heat repeats. Pds5 also promotes the acetylation of Smc3 that protects cohesin from releasing activity in G2 phase.


Pssm-ID: 410996 [Multi-domain]  Cd Length: 630  Bit Score: 58.69  E-value: 8.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 258 AIPELLKA--------LEDSNKDVRIKAAEALGKIGSETAITGL-----------LKALKDSNSIVRIKAAKALGNI--- 315
Cdd:cd19953   238 IAPELLLSvipqleeeLKADDVDVRLLATKLLGKMFAEKGSAGFaqtypslwkefLGRFNDKSPEVRLAWVESAKHIlln 317

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733579917 316 ---GSETVIPGLLKALEDSDRYVRRDAAQALGKISSETAIAG----LLKAL----KDSYFSVRWKAVEALGKI 377
Cdd:cd19953   318 hpdLAEDILEALKKRLLDPDEKVRLAAVKAICDLAYEDLLHKvpeeLLSTLaerlRDKKASVRKEALQGLARL 390
TIR smart00255
Toll - interleukin 1 - resistance;
493-608 2.08e-07

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 50.78  E-value: 2.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  493 QVYISYNWQEDS-NEMANQLVQAFDAKGIEI-IRDKTHtsYKDSIKNFMRQIGRGKCVVAVISDRYLKSENCMFELVEIA 570
Cdd:smart00255   3 DVFISYSGKEDVrNEFLSHLLEKLRGYGLCVfIDDFEP--GGGDLEEIDEAIEKSRIAIVVLSPNYAESEWCLDELVAAL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1733579917  571 RN--GDFYKRIFPIIL---------PDARIYKDFeRIDYLKYWEDEKAK 608
Cdd:smart00255  81 ENalEEGGLRVIPIFYevipsdvrkQPGKFRKVF-KKNYLKWPEDEKEQ 128
EZ_HEAT smart00567
E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other ...
 240-269 6.59e-07

E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other proteins. Probable scaffolding role.


Pssm-ID: 128837 [Multi-domain]  Cd Length: 30  Bit Score: 45.87  E-value: 6.59e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 1733579917  240 WSVRRNAAFALAEIGTETAIPELLKALEDS 269
Cdd:smart00567   1 PLVRHEAAFALGQLGDEEAVPALIKALEDE 30
EZ_HEAT smart00567
E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other ...
 53-82 1.10e-05

E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other proteins. Probable scaffolding role.


Pssm-ID: 128837 [Multi-domain]  Cd Length: 30  Bit Score: 42.40  E-value: 1.10e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1733579917   53 EYVRRSAAFALGKIGSETAIGGLLKALEDS 82
Cdd:smart00567   1 PLVRHEAAFALGQLGDEEAVPALIKALEDE 30
EZ_HEAT smart00567
E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other ...
 365-393 1.20e-05

E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other proteins. Probable scaffolding role.


Pssm-ID: 128837 [Multi-domain]  Cd Length: 30  Bit Score: 42.40  E-value: 1.20e-05
                           10        20
                   ....*....|....*....|....*....
gi 1733579917  365 SVRWKAVEALGKIGSETAIPGLLKALEDS 393
Cdd:smart00567   2 LVRHEAAFALGQLGDEEAVPALIKALEDE 30
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 152-193 6.86e-05

Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; Epoxyqueuosine reductase QueG (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441208 [Multi-domain]  Cd Length: 345  Bit Score: 45.58  E-value: 6.86e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1733579917 152 AAYALGNISSETAIAGLLKALEHSNSDVRGYAAFALGKIGSE 193
Cdd:COG1600   303 AAIALGNSGDPAAVPALEALLDDPSPLVREHAAWALGRLGGR 344
EZ_HEAT smart00567
E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other ...
 179-206 1.11e-04

E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other proteins. Probable scaffolding role.


Pssm-ID: 128837 [Multi-domain]  Cd Length: 30  Bit Score: 39.71  E-value: 1.11e-04
                           10        20
                   ....*....|....*....|....*...
gi 1733579917  179 VRGYAAFALGKIGSETAIGGLLKALEDS 206
Cdd:smart00567   3 VRHEAAFALGQLGDEEAVPALIKALEDE 30
PRK09687 PRK09687
putative lyase; Provisional
 297-437 6.97e-04

putative lyase; Provisional


Pssm-ID: 170047 [Multi-domain]  Cd Length: 280  Bit Score: 42.04  E-value: 6.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 297 LKDSNSIVRIKAAKALGNIGSETVIPGLLKALEDSDRYVRRDAAQALGKIS----SETAIAGLLKAL--KDSYFSVRWKA 370
Cdd:PRK09687   32 LDDHNSLKRISSIRVLQLRGGQDVFRLAIELCSSKNPIERDIGADILSQLGmakrCQDNVFNILNNLalEDKSACVRASA 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733579917 371 VEALG------KIGSETAIPGLLKALEDSNSILRWKAAEALGNIGSETAIPGLLKALEHSNSNVRVYAAVALG 437
Cdd:PRK09687  112 INATGhrckknPLYSPKIVEQSQITAFDKSTNVRFAVAFALSVINDEAAIPLLINLLKDPNGDVRNWAAFALN 184
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 1-38 6.01e-03

Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; Epoxyqueuosine reductase QueG (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441208 [Multi-domain]  Cd Length: 345  Bit Score: 39.42  E-value: 6.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1733579917   1 MGNISSETAIAGLLKALEHSNSDVRGYAAFALGKIGSE 38
Cdd:COG1600   307 LGNSGDPAAVPALEALLDDPSPLVREHAAWALGRLGGR 344
HEAT_PBS pfam03130
PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to ...
 428-454 8.78e-03

PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to pfam02985. Cyanobacteria and red algae harvest light energy using macromolecular complexes known as phycobilisomes (PBS), peripherally attached to the photosynthetic membrane. The major components of PBS are the phycobiliproteins. These heterodimeric proteins are covalently attached to phycobilins: open-chain tetrapyrrole chromophores, which function as the photosynthetic light-harvesting pigments. Phycobiliproteins differ in sequence and in the nature and number of attached phycobilins to each of their subunits. This family includes the lyase enzymes that specifically attach particular phycobilins to apophycobiliprotein subunits. The most comprehensively studied of these is the CpcE/F lyase, which attaches phycocyanobilin (PCB) to the alpha subunit of apophycocyanin. Similarly, MpeU/V attaches phycoerythrobilin to phycoerythrin II, while CpeY/Z is thought to be involved in phycoerythrobilin (PEB) attachment to phycoerythrin (PE) I (PEs I and II differ in sequence and in the number of attached molecules of PEB: PE I has five, PE II has six). All the reactions of the above lyases involve an apoprotein cysteine SH addition to a terminal delta 3,3'-double bond. Such a reaction is not possible in the case of phycoviolobilin (PVB), the phycobilin of alpha-phycoerythrocyanin (alpha-PEC). It is thought that in this case, PCB, not PVB, is first added to apo-alpha-PEC, and is then isomerized to PVB. The addition reaction has been shown to occur in the presence of either of the components of alpha-PEC-PVB lyase PecE or PecF (or both). The isomerization reaction occurs only when both PecE and PecF components are present, i.e. the PecE/F phycobiliprotein lyase is also a phycobilin isomerase. Another member of this family is the NblB protein, whose similarity to the phycobiliprotein lyases was previously noted. This constitutively expressed protein is not known to have any lyase activity. It is thought to be involved in the coordination of PBS degradation with environmental nutrient limitation. It has been suggested that the similarity of NblB to the phycobiliprotein lyases is due to the ability to bind tetrapyrrole phycobilins via the common repeated motif.


Pssm-ID: 308641 [Multi-domain]  Cd Length: 27  Bit Score: 34.38  E-value: 8.78e-03
                          10        20
                  ....*....|....*....|....*..
gi 1733579917 428 VRVYAAVALGKIGTEAAMTELIKCLKN 454
Cdd:pfam03130   1 VRRAAARALGALGDPEAIPALIEALDD 27
 
Name Accession Description Interval E-value
HEAT COG1413
HEAT repeat [General function prediction only];
210-346 2.84e-42

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 149.78  E-value: 2.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 210 VRRNAAFALGNIGSETAIQELLKALEDsDDWSVRRNAAFALAEIGTETAIPELLKALEDSNKDVRIKAAEALGKIGSETA 289
Cdd:COG1413     1 VRRAAARALGRLGDPAAVPALIAALAD-EDPDVRAAAARALGRLGDPRAVPALLEALKDPDPEVRAAAAEALGRIGDPEA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1733579917 290 ITGLLKALKDSNSIVRIKAAKALGNIGSETVIPGLLKALEDSDRYVRRDAAQALGKI 346
Cdd:COG1413    80 VPALIAALKDEDPEVRRAAAEALGRLGDPAAVPALLEALKDPDWEVRRAAARALGRL 136
HEAT COG1413
HEAT repeat [General function prediction only];
179-316 4.58e-42

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 149.39  E-value: 4.58e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 179 VRGYAAFALGKIGSETAIGGLLKALEDSDEYVRRNAAFALGNIGSETAIQELLKALEDsDDWSVRRNAAFALAEIGTETA 258
Cdd:COG1413     1 VRRAAARALGRLGDPAAVPALIAALADEDPDVRAAAARALGRLGDPRAVPALLEALKD-PDPEVRAAAAEALGRIGDPEA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1733579917 259 IPELLKALEDSNKDVRIKAAEALGKIGSETAITGLLKALKDSNSIVRIKAAKALGNIG 316
Cdd:COG1413    80 VPALIAALKDEDPEVRRAAAEALGRLGDPAAVPALLEALKDPDWEVRRAAARALGRLG 137
HEAT COG1413
HEAT repeat [General function prediction only];
242-378 2.12e-41

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 147.47  E-value: 2.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 242 VRRNAAFALAEIGTETAIPELLKALEDSNKDVRIKAAEALGKIGSETAITGLLKALKDSNSIVRIKAAKALGNIGSETVI 321
Cdd:COG1413     1 VRRAAARALGRLGDPAAVPALIAALADEDPDVRAAAARALGRLGDPRAVPALLEALKDPDPEVRAAAAEALGRIGDPEAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1733579917 322 PGLLKALEDSDRYVRRDAAQALGKISSETAIAGLLKALKDSYFSVRWKAVEALGKIG 378
Cdd:COG1413    81 PALIAALKDEDPEVRRAAAEALGRLGDPAAVPALLEALKDPDWEVRRAAARALGRLG 137
HEAT COG1413
HEAT repeat [General function prediction only];
148-285 3.67e-41

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 146.70  E-value: 3.67e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 148 VREYAAYALGNISSETAIAGLLKALEHSNSDVRGYAAFALGKIGSETAIGGLLKALEDSDEYVRRNAAFALGNIGSETAI 227
Cdd:COG1413     1 VRRAAARALGRLGDPAAVPALIAALADEDPDVRAAAARALGRLGDPRAVPALLEALKDPDPEVRAAAAEALGRIGDPEAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1733579917 228 QELLKALEDsDDWSVRRNAAFALAEIGTETAIPELLKALEDSNKDVRIKAAEALGKIG 285
Cdd:COG1413    81 PALIAALKD-EDPEVRRAAAEALGRLGDPAAVPALLEALKDPDWEVRRAAARALGRLG 137
HEAT COG1413
HEAT repeat [General function prediction only];
24-159 9.73e-41

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 145.54  E-value: 9.73e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  24 VRGYAAFALGKIGSETAIGGLLKALEDSDEYVRRSAAFALGKIGSETAIGGLLKALEDSDEYVRMYAAKALGNIGSETAI 103
Cdd:COG1413     1 VRRAAARALGRLGDPAAVPALIAALADEDPDVRAAAARALGRLGDPRAVPALLEALKDPDPEVRAAAAEALGRIGDPEAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1733579917 104 TGLLKALEDSDEDVLWNAAEALGKIGTETTIAGLLKALEDSNKDVREYAAYALGNI 159
Cdd:COG1413    81 PALIAALKDEDPEVRRAAAEALGRLGDPAAVPALLEALKDPDWEVRRAAARALGRL 136
HEAT COG1413
HEAT repeat [General function prediction only];
86-222 1.03e-40

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 145.54  E-value: 1.03e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  86 VRMYAAKALGNIGSETAITGLLKALEDSDEDVLWNAAEALGKIGTETTIAGLLKALEDSNKDVREYAAYALGNISSETAI 165
Cdd:COG1413     1 VRRAAARALGRLGDPAAVPALIAALADEDPDVRAAAARALGRLGDPRAVPALLEALKDPDPEVRAAAAEALGRIGDPEAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1733579917 166 AGLLKALEHSNSDVRGYAAFALGKIGSETAIGGLLKALEDSDEYVRRNAAFALGNIG 222
Cdd:COG1413    81 PALIAALKDEDPEVRRAAAEALGRLGDPAAVPALLEALKDPDWEVRRAAARALGRLG 137
HEAT COG1413
HEAT repeat [General function prediction only];
55-191 1.65e-40

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 144.77  E-value: 1.65e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  55 VRRSAAFALGKIGSETAIGGLLKALEDSDEYVRMYAAKALGNIGSETAITGLLKALEDSDEDVLWNAAEALGKIGTETTI 134
Cdd:COG1413     1 VRRAAARALGRLGDPAAVPALIAALADEDPDVRAAAARALGRLGDPRAVPALLEALKDPDPEVRAAAAEALGRIGDPEAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1733579917 135 AGLLKALEDSNKDVREYAAYALGNISSETAIAGLLKALEHSNSDVRGYAAFALGKIG 191
Cdd:COG1413    81 PALIAALKDEDPEVRRAAAEALGRLGDPAAVPALLEALKDPDWEVRRAAARALGRLG 137
HEAT COG1413
HEAT repeat [General function prediction only];
304-440 1.71e-40

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 144.77  E-value: 1.71e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 304 VRIKAAKALGNIGSETVIPGLLKALEDSDRYVRRDAAQALGKISSETAIAGLLKALKDSYFSVRWKAVEALGKIGSETAI 383
Cdd:COG1413     1 VRRAAARALGRLGDPAAVPALIAALADEDPDVRAAAARALGRLGDPRAVPALLEALKDPDPEVRAAAAEALGRIGDPEAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1733579917 384 PGLLKALEDSNSILRWKAAEALGNIGSETAIPGLLKALEHSNSNVRVYAAVALGKIG 440
Cdd:COG1413    81 PALIAALKDEDPEVRRAAAEALGRLGDPAAVPALLEALKDPDWEVRRAAARALGRLG 137
HEAT COG1413
HEAT repeat [General function prediction only];
273-409 2.26e-40

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 144.39  E-value: 2.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 273 VRIKAAEALGKIGSETAITGLLKALKDSNSIVRIKAAKALGNIGSETVIPGLLKALEDSDRYVRRDAAQALGKISSETAI 352
Cdd:COG1413     1 VRRAAARALGRLGDPAAVPALIAALADEDPDVRAAAARALGRLGDPRAVPALLEALKDPDPEVRAAAAEALGRIGDPEAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1733579917 353 AGLLKALKDSYFSVRWKAVEALGKIGSETAIPGLLKALEDSNSILRWKAAEALGNIG 409
Cdd:COG1413    81 PALIAALKDEDPEVRRAAAEALGRLGDPAAVPALLEALKDPDWEVRRAAARALGRLG 137
HEAT COG1413
HEAT repeat [General function prediction only];
120-254 3.53e-39

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 141.30  E-value: 3.53e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 120 NAAEALGKIGTETTIAGLLKALEDSNKDVREYAAYALGNISSETAIAGLLKALEHSNSDVRGYAAFALGKIGSETAIGGL 199
Cdd:COG1413     4 AAARALGRLGDPAAVPALIAALADEDPDVRAAAARALGRLGDPRAVPALLEALKDPDPEVRAAAAEALGRIGDPEAVPAL 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1733579917 200 LKALEDSDEYVRRNAAFALGNIGSETAIQELLKALEDsDDWSVRRNAAFALAEIG 254
Cdd:COG1413    84 IAALKDEDPEVRRAAAEALGRLGDPAAVPALLEALKD-PDWEVRRAAARALGRLG 137
HEAT COG1413
HEAT repeat [General function prediction only];
1-129 3.81e-37

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 135.53  E-value: 3.81e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917   1 MGNISSETAIAGLLKALEHSNSDVRGYAAFALGKIGSETAIGGLLKALEDSDEYVRRSAAFALGKIGSETAIGGLLKALE 80
Cdd:COG1413     9 LGRLGDPAAVPALIAALADEDPDVRAAAARALGRLGDPRAVPALLEALKDPDPEVRAAAAEALGRIGDPEAVPALIAALK 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1733579917  81 DSDEYVRMYAAKALGNIGSETAITGLLKALEDSDEDVLWNAAEALGKIG 129
Cdd:COG1413    89 DEDPEVRRAAAEALGRLGDPAAVPALLEALKDPDWEVRRAAARALGRLG 137
HEAT COG1413
HEAT repeat [General function prediction only];
335-456 3.31e-33

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 124.36  E-value: 3.31e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 335 VRRDAAQALGKISSETAIAGLLKALKDSYFSVRWKAVEALGKIGSETAIPGLLKALEDSNSILRWKAAEALGNIGSETAI 414
Cdd:COG1413     1 VRRAAARALGRLGDPAAVPALIAALADEDPDVRAAAARALGRLGDPRAVPALLEALKDPDPEVRAAAAEALGRIGDPEAV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1733579917 415 PGLLKALEHSNSNVRVYAAVALGKIGTEAAMTELIKCLKNPD 456
Cdd:COG1413    81 PALIAALKDEDPEVRRAAAEALGRLGDPAAVPALLEALKDPD 122
PRK13800 PRK13800
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
162-436 1.09e-22

fumarate reductase/succinate dehydrogenase flavoprotein subunit;


Pssm-ID: 237512 [Multi-domain]  Cd Length: 897  Bit Score: 103.78  E-value: 1.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 162 ETAIAGLLKALEHSNSDVRGYAAFALGKIGSETAIGGLLKALEDSDEYVRRNAAFALGNI----GSETAIQELLkaleDS 237
Cdd:PRK13800  620 APSVAELAPYLADPDPGVRRTAVAVLTETTPPGFGPALVAALGDGAAAVRRAAAEGLRELvevlPPAPALRDHL----GS 695

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 238 DDWSVRRNAAFALAEIGTETAIpELLKALEDSNKDVRIKAAEALGkigSETAITGLLKALKDSNSIVRIKAAKALGNIGS 317
Cdd:PRK13800  696 PDPVVRAAALDVLRALRAGDAA-LFAAALGDPDHRVRIEAVRALV---SVDDVESVAGAATDENREVRIAVAKGLATLGA 771

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 318 ETVIPG-LLKAL-EDSDRYVRRDAAQALGKISSETAIAG-LLKALKDSYFSVRWKAVEALGKIGSETAIPGLLKALEDSN 394
Cdd:PRK13800  772 GGAPAGdAVRALtGDPDPLVRAAALAALAELGCPPDDVAaATAALRASAWQVRQGAARALAGAAADVAVPALVEALTDPH 851

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1733579917 395 SILRWKAAEALGNI-GSETAIPGLLKALEHSNSNVRVYAAVAL 436
Cdd:PRK13800  852 LDVRKAAVLALTRWpGDPAARDALTTALTDSDADVRAYARRAL 894
PRK13800 PRK13800
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
44-312 1.58e-22

fumarate reductase/succinate dehydrogenase flavoprotein subunit;


Pssm-ID: 237512 [Multi-domain]  Cd Length: 897  Bit Score: 103.39  E-value: 1.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  44 LLKALEDSDEYVRRSAAFALGKIGSETAIGGLLKALEDSDEYVRMYAAKALGNI----GSETAITGLLkaleDSDEDVLW 119
Cdd:PRK13800  626 LAPYLADPDPGVRRTAVAVLTETTPPGFGPALVAALGDGAAAVRRAAAEGLRELvevlPPAPALRDHL----GSPDPVVR 701

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 120 NAAEALGKIGTETTIAGLLKALEDSNKDVREYAAYALgniSSETAIAGLLKALEHSNSDVRGYAAFALGKIGSETAIGG- 198
Cdd:PRK13800  702 AAALDVLRALRAGDAALFAAALGDPDHRVRIEAVRAL---VSVDDVESVAGAATDENREVRIAVAKGLATLGAGGAPAGd 778

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 199 LLKAL-EDSDEYVRRNAAFALGNIGSETAIQELLKALEDSDDWSVRRNAAFALAEIGTETAIPELLKALEDSNKDVRIKA 277
Cdd:PRK13800  779 AVRALtGDPDPLVRAAALAALAELGCPPDDVAAATAALRASAWQVRQGAARALAGAAADVAVPALVEALTDPHLDVRKAA 858

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1733579917 278 AEALGKI-GSETAITGLLKALKDSNSIVRIKAAKAL 312
Cdd:PRK13800  859 VLALTRWpGDPAARDALTTALTDSDADVRAYARRAL 894
PRK13800 PRK13800
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
131-405 1.92e-21

fumarate reductase/succinate dehydrogenase flavoprotein subunit;


Pssm-ID: 237512 [Multi-domain]  Cd Length: 897  Bit Score: 99.92  E-value: 1.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 131 ETTIAGLLKALEDSNKDVREYAAYALGNISSETAIAGLLKALEHSNSDVRGYAAFALGKI----GSETAIGGLLKAledS 206
Cdd:PRK13800  620 APSVAELAPYLADPDPGVRRTAVAVLTETTPPGFGPALVAALGDGAAAVRRAAAEGLRELvevlPPAPALRDHLGS---P 696

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 207 DEYVRRNAAFALGNIGSETAIQeLLKALEDSDDwSVRRNAAFALAEIgteTAIPELLKALEDSNKDVRIKAAEALGKIGS 286
Cdd:PRK13800  697 DPVVRAAALDVLRALRAGDAAL-FAAALGDPDH-RVRIEAVRALVSV---DDVESVAGAATDENREVRIAVAKGLATLGA 771

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 287 ETAI-TGLLKAL-KDSNSIVRIKAAKALGNIGSETVIPG-LLKALEDSDRYVRRDAAQALGKISSETAIAGLLKALKDSY 363
Cdd:PRK13800  772 GGAPaGDAVRALtGDPDPLVRAAALAALAELGCPPDDVAaATAALRASAWQVRQGAARALAGAAADVAVPALVEALTDPH 851

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1733579917 364 FSVRWKAVEALGKI-GSETAIPGLLKALEDSNSILRWKAAEAL 405
Cdd:PRK13800  852 LDVRKAAVLALTRWpGDPAARDALTTALTDSDADVRAYARRAL 894
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 227-313 3.27e-21

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 88.55  E-value: 3.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 227 IQELLKALEDSDDWSVRRNAAFALAEIGTETAIPELLKALEDSNKDVRIKAAEALGKIGSETAITGLLKALK-DSNSIVR 305
Cdd:pfam13646   1 LPALLQALLRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDEDPAVRRAAAEALGKIGDPEALPALLELLRdDDDDVVR 80


                  ....*...
gi 1733579917 306 IKAAKALG 313
Cdd:pfam13646  81 AAAAEALA 88
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 259-344 1.10e-19

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 83.93  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 259 IPELLKAL-EDSNKDVRIKAAEALGKIGSETAITGLLKALKDSNSIVRIKAAKALGNIGSETVIPGLLKAL-EDSDRYVR 336
Cdd:pfam13646   1 LPALLQALlRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDEDPAVRRAAAEALGKIGDPEALPALLELLrDDDDDVVR 80


                  ....*...
gi 1733579917 337 RDAAQALG 344
Cdd:pfam13646  81 AAAAEALA 88
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 165-251 2.96e-19

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 82.77  E-value: 2.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 165 IAGLLKAL-EHSNSDVRGYAAFALGKIGSETAIGGLLKALEDSDEYVRRNAAFALGNIGSETAIQELLKALEDSDDWSVR 243
Cdd:pfam13646   1 LPALLQALlRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDEDPAVRRAAAEALGKIGDPEALPALLELLRDDDDDVVR 80


                  ....*...
gi 1733579917 244 RNAAFALA 251
Cdd:pfam13646  81 AAAAEALA 88
PRK13800 PRK13800
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
199-473 3.44e-18

fumarate reductase/succinate dehydrogenase flavoprotein subunit;


Pssm-ID: 237512 [Multi-domain]  Cd Length: 897  Bit Score: 89.14  E-value: 3.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 199 LLKALEDSDEYVRRNAAFALGNIGSETAIQELLKALEDsDDWSVRRNAAFALAEIgTETAIPE--LLKALEDSNKDVRIK 276
Cdd:PRK13800  626 LAPYLADPDPGVRRTAVAVLTETTPPGFGPALVAALGD-GAAAVRRAAAEGLREL-VEVLPPApaLRDHLGSPDPVVRAA 703

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 277 AAEALGKIGSETAITgLLKALKDSNSIVRIKAAKALGNIGSETvipGLLKALEDSDRYVRRDAAQALGKISSETAIAG-L 355
Cdd:PRK13800  704 ALDVLRALRAGDAAL-FAAALGDPDHRVRIEAVRALVSVDDVE---SVAGAATDENREVRIAVAKGLATLGAGGAPAGdA 779

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 356 LKAL-KDSYFSVRWKAVEALGKIGSETAIPG-LLKALEDSNSILRWKAAEALGNIGSETAIPGLLKALEHSNSNVRVYAA 433
Cdd:PRK13800  780 VRALtGDPDPLVRAAALAALAELGCPPDDVAaATAALRASAWQVRQGAARALAGAAADVAVPALVEALTDPHLDVRKAAV 859

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1733579917 434 VALGKI-GTEAAMTELIKCLKNPDfvtlnnGDTLFQARKAL 473
Cdd:PRK13800  860 LALTRWpGDPAARDALTTALTDSD------ADVRAYARRAL 894
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 199-282 7.56e-18

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 78.92  E-value: 7.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 199 LLKAL-EDSDEYVRRNAAFALGNIGSETAIQELLKALEDsDDWSVRRNAAFALAEIGTETAIPELLKAL-EDSNKDVRIK 276
Cdd:pfam13646   4 LLQALlRDPDPEVRAAAIRALGRIGDPEAVPALLELLKD-EDPAVRRAAAEALGKIGDPEALPALLELLrDDDDDVVRAA 82


                  ....*.
gi 1733579917 277 AAEALG 282
Cdd:pfam13646  83 AAEALA 88
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 321-406 9.74e-18

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 78.53  E-value: 9.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 321 IPGLLKAL-EDSDRYVRRDAAQALGKISSETAIAGLLKALKDSYFSVRWKAVEALGKIGSETAIPGLLKAL-EDSNSILR 398
Cdd:pfam13646   1 LPALLQALlRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDEDPAVRRAAAEALGKIGDPEALPALLELLrDDDDDVVR 80


                  ....*...
gi 1733579917 399 WKAAEALG 406
Cdd:pfam13646  81 AAAAEALA 88
PRK13800 PRK13800
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
106-374 2.50e-17

fumarate reductase/succinate dehydrogenase flavoprotein subunit;


Pssm-ID: 237512 [Multi-domain]  Cd Length: 897  Bit Score: 86.44  E-value: 2.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 106 LLKALEDSDEDVLWNAAEALGKIGTETTIAGLLKALEDSNKDVREYAAYALGNI----SSETAIAGLLKAlehSNSDVRG 181
Cdd:PRK13800  626 LAPYLADPDPGVRRTAVAVLTETTPPGFGPALVAALGDGAAAVRRAAAEGLRELvevlPPAPALRDHLGS---PDPVVRA 702

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 182 YAAFALGKIGSETAiGGLLKALEDSDEYVRRNAAFALGnigSETAIQELLKALEDSDDwSVRRNAAFALAEI--GTETAI 259
Cdd:PRK13800  703 AALDVLRALRAGDA-ALFAAALGDPDHRVRIEAVRALV---SVDDVESVAGAATDENR-EVRIAVAKGLATLgaGGAPAG 777

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 260 PELLKALEDSNKDVRIKAAEALGKIGSETAITG-LLKALKDSNSIVRIKAAKALGNIGSETVIPGLLKALEDSDRYVRRD 338
Cdd:PRK13800  778 DAVRALTGDPDPLVRAAALAALAELGCPPDDVAaATAALRASAWQVRQGAARALAGAAADVAVPALVEALTDPHLDVRKA 857

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1733579917 339 AAQALGKISSETAIA-GLLKALKDSYFSVRWKAVEAL 374
Cdd:PRK13800  858 AVLALTRWPGDPAARdALTTALTDSDADVRAYARRAL 894
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 44-126 4.07e-17

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 76.61  E-value: 4.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  44 LLKAL-EDSDEYVRRSAAFALGKIGSETAIGGLLKALEDSDEYVRMYAAKALGNIGSETAITGLLKAL-EDSDEDVLWNA 121
Cdd:pfam13646   4 LLQALlRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDEDPAVRRAAAEALGKIGDPEALPALLELLrDDDDDVVRAAA 83


                  ....*
gi 1733579917 122 AEALG 126
Cdd:pfam13646  84 AEALA 88
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 75-157 4.58e-17

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 76.61  E-value: 4.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  75 LLKAL-EDSDEYVRMYAAKALGNIGSETAITGLLKALEDSDEDVLWNAAEALGKIGTETTIAGLLKAL-EDSNKDVREYA 152
Cdd:pfam13646   4 LLQALlRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDEDPAVRRAAAEALGKIGDPEALPALLELLrDDDDDVVRAAA 83


                  ....*
gi 1733579917 153 AYALG 157
Cdd:pfam13646  84 AEALA 88
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 10-95 5.05e-17

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 76.61  E-value: 5.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  10 IAGLLKAL-EHSNSDVRGYAAFALGKIGSETAIGGLLKALEDSDEYVRRSAAFALGKIGSETAIGGLLKAL-EDSDEYVR 87
Cdd:pfam13646   1 LPALLQALlRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDEDPAVRRAAAEALGKIGDPEALPALLELLrDDDDDVVR 80


                  ....*...
gi 1733579917  88 MYAAKALG 95
Cdd:pfam13646  81 AAAAEALA 88
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 290-375 1.53e-16

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 75.07  E-value: 1.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 290 ITGLLKAL-KDSNSIVRIKAAKALGNIGSETVIPGLLKALEDSDRYVRRDAAQALGKISSETAIAGLLKALK-DSYFSVR 367
Cdd:pfam13646   1 LPALLQALlRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDEDPAVRRAAAEALGKIGDPEALPALLELLRdDDDDVVR 80


                  ....*...
gi 1733579917 368 WKAVEALG 375
Cdd:pfam13646  81 AAAAEALA 88
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 352-435 4.26e-16

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 73.91  E-value: 4.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 352 IAGLLKAL-KDSYFSVRWKAVEALGKIGSETAIPGLLKALEDSNSILRWKAAEALGNIGSETAIPGLLKALEHSNSNVRV 430
Cdd:pfam13646   1 LPALLQALlRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDEDPAVRRAAAEALGKIGDPEALPALLELLRDDDDDVVR 80


                  ....*
gi 1733579917 431 YAAVA 435
Cdd:pfam13646  81 AAAAE 85
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 134-219 9.56e-16

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 72.76  E-value: 9.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 134 IAGLLKAL-EDSNKDVREYAAYALGNISSETAIAGLLKALEHSNSDVRGYAAFALGKIGSETAIGGLLKAL-EDSDEYVR 211
Cdd:pfam13646   1 LPALLQALlRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDEDPAVRRAAAEALGKIGDPEALPALLELLrDDDDDVVR 80


                  ....*...
gi 1733579917 212 RNAAFALG 219
Cdd:pfam13646  81 AAAAEALA 88
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 103-188 2.36e-14

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 68.90  E-value: 2.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 103 ITGLLKAL-EDSDEDVLWNAAEALGKIGTETTIAGLLKALEDSNKDVREYAAYALGNISSETAIAGLLKALEHSNSD-VR 180
Cdd:pfam13646   1 LPALLQALlRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDEDPAVRRAAAEALGKIGDPEALPALLELLRDDDDDvVR 80


                  ....*...
gi 1733579917 181 GYAAFALG 188
Cdd:pfam13646  81 AAAAEALA 88
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 383-456 6.82e-14

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 67.36  E-value: 6.82e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1733579917 383 IPGLLKAL-EDSNSILRWKAAEALGNIGSETAIPGLLKALEHSNSNVRVYAAVALGKIGTEAAMTELIKCLKNPD 456
Cdd:pfam13646   1 LPALLQALlRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDEDPAVRRAAAEALGKIGDPEALPALLELLRDDD 75
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
 494-606 2.89e-13

TIR domain; This is a family of Toll-like receptors.


Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 66.57  E-value: 2.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 494 VYISYNWqEDSnEMANQLVQAFDAKGIEIIRDKTHTSYKDSIKNFMRQ-IGRGKCVVAVISDRYLKSENCMFELVEIARN 572
Cdd:pfam13676   1 VFISYAG-EDR-AWAEWLADALEAAGYRVWLDRWDIRPGDDWVEEIEEaIENSDRVLVVLSPNYLESPWCRAEWEAALAD 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1733579917 573 GDFYKRIFPIILPDARIYKDFERIDYLKYWEDEK 606
Cdd:pfam13676  79 PEGRKRLIPVRLECDLELPGLAGLQYIDLRDGDE 112
PRK13800 PRK13800
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
11-251 5.94e-13

fumarate reductase/succinate dehydrogenase flavoprotein subunit;


Pssm-ID: 237512 [Multi-domain]  Cd Length: 897  Bit Score: 72.58  E-value: 5.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  11 AGLLKALEHSNSDVRGYAAFALGKI----GSETAIGGLLkaleDSDEYVRRSAAFALGKIGSETAIGGLLKALEDSDEYV 86
Cdd:PRK13800  655 PALVAALGDGAAAVRRAAAEGLRELvevlPPAPALRDHL----GSPDPVVRAAALDVLRALRAGDAALFAAALGDPDHRV 730

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  87 RMYAAKALGNIGSETAITGllkALEDSDEDVLWNAAEALGKIGTET-TIAGLLKAL-EDSNKDVREYAAYALGNISSETA 164
Cdd:PRK13800  731 RIEAVRALVSVDDVESVAG---AATDENREVRIAVAKGLATLGAGGaPAGDAVRALtGDPDPLVRAAALAALAELGCPPD 807

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 165 IAG-LLKALEHSNSDVRGYAAFALGKIGSETAIGGLLKALEDSDEYVRRNAAFALGNI-GSETAIQELLKALEDSDDwSV 242
Cdd:PRK13800  808 DVAaATAALRASAWQVRQGAARALAGAAADVAVPALVEALTDPHLDVRKAAVLALTRWpGDPAARDALTTALTDSDA-DV 886


                  ....*....
gi 1733579917 243 RRNAAFALA 251
Cdd:PRK13800  887 RAYARRALA 895
PRK09687 PRK09687
putative lyase; Provisional
 48-284 7.07e-12

putative lyase; Provisional


Pssm-ID: 170047 [Multi-domain]  Cd Length: 280  Bit Score: 66.69  E-value: 7.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  48 LEDSDEYVRRSAAFALGKIGSETAIGGLLKALEDSDEYVRMYAAKALGNIG----SETAITGLLKAL--EDSDEDVLWNA 121
Cdd:PRK09687   32 LDDHNSLKRISSIRVLQLRGGQDVFRLAIELCSSKNPIERDIGADILSQLGmakrCQDNVFNILNNLalEDKSACVRASA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 122 AEALG------KIGTETTIAGLLKALEDSNKDVREYAAYALGNISSETAIAGLLKALEHSNSDVRGYAAFALG--KIGSE 193
Cdd:PRK09687  112 INATGhrckknPLYSPKIVEQSQITAFDKSTNVRFAVAFALSVINDEAAIPLLINLLKDPNGDVRNWAAFALNsnKYDNP 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 194 TAIGGLLKALEDSDEYVRRNAAFALGNIGSETAIQELLKALEDSDdwsVRRNAAFALAEIGTETAIPELLKALEDSNkDV 273
Cdd:PRK09687  192 DIREAFVAMLQDKNEEIRIEAIIGLALRKDKRVLSVLIKELKKGT---VGDLIIEAAGELGDKTLLPVLDTLLYKFD-DN 267

                         250
                  ....*....|...
gi 1733579917 274 RI--KAAEALGKI 284
Cdd:PRK09687  268 EIitKAIDKLKRS 280
PDS5 pfam20168
Sister chromatid cohesion protein PDS5 protein; This entry represents the Sister chromatid ...
 258-377 3.12e-10

Sister chromatid cohesion protein PDS5 protein; This entry represents the Sister chromatid cohesion protein PDS5. The large PDS5 molecule is exclusively alpha helical, composed of a large number of HEAT-like repeats and helical extensions/additions that deviate from the HEAT repeat pattern.


Pssm-ID: 466319 [Multi-domain]  Cd Length: 1051  Bit Score: 63.77  E-value: 3.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  258 AIPELLKA--------LEDSNKDVRIKAAEALGKIGSETAITGL-----------LKALKDSNSIVRIKAAKALGNI--- 315
Cdd:pfam20168  235 IAPSLLLNvipqleeeLKADDVDIRLLATETLGRMFSEPGGSDLakqypslwkawLGRFNDKSVAVRIAWVEAAKQIlln 314

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733579917  316 ---GSETVIPGLLKALEDSDRYVRRDAAQALGKISSETAIA----GLLKAL----KDSYFSVRWKAVEALGKI 377
Cdd:pfam20168  315 hpdLRSEILEALKDRLLDPDEKVRLAAVKAIGDLDYETLLHvvseKLLKTLaerlRDKKPSVRKEALKTLAKL 387
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 1-64 1.85e-09

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 55.04  E-value: 1.85e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1733579917   1 MGNISSETAIAGLLKALEHSNSDVRGYAAFALGKIGSETAIGGLLKAL-EDSDEYVRRSAAFALG 64
Cdd:pfam13646  24 LGRIGDPEAVPALLELLKDEDPAVRRAAAEALGKIGDPEALPALLELLrDDDDDVVRAAAAEALA 88
RPN2 COG5116
26S proteasome regulatory complex component [Posttranslational modification, protein turnover, ...
 124-346 2.68e-09

26S proteasome regulatory complex component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227446 [Multi-domain]  Cd Length: 926  Bit Score: 60.73  E-value: 2.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 124 ALGKI----GTETT--IAGLLKALEDSNKDVREYAA-YALGNI---SSETAIAGLLKALEHSNSDVRGYAA-FALGKIGS 192
Cdd:COG5116   396 ALGLIkagfGREDTeyLLEYFLDTEDELTPELAYGVcLGIGLInmgSANREIYEKLKELLKNDRALLGEAAvYGMGLLML 475

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 193 ETAIGGLLKAL-----EDSDEYVRRNAA--FALGNIGSETAIQELLKALEDSDDWSVRRNAAF--ALAEIGT--ETAIPE 261
Cdd:COG5116   476 GTWSVEAIEDMrtyagETQHERIKRGLGigFALILYGRQEMADDYINELLYDKDSILRYNGVFslALAYVGTgnLGVVST 555

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 262 LLK-ALEDSNKDVRIKAAEALGKI--GSETAITGLLKALKDS-NSIVRIKAAKALG----NIGSETVIPGLLKALEDSDR 333
Cdd:COG5116   556 LLHyAVSDGNDDVRRAAVIALGFVccDDRDLLVGTVELLSEShNFHVRAGVAVALGiacaGTGDKVATDILEALMYDTND 635

                         250
                  ....*....|...
gi 1733579917 334 YVRRDAAQALGKI 346
Cdd:COG5116   636 FVRQSAMIAVGMI 648
Adaptin_N pfam01602
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
 164-429 8.07e-09

Adaptin N terminal region; This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles.


Pssm-ID: 396262 [Multi-domain]  Cd Length: 523  Bit Score: 58.79  E-value: 8.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 164 AIAGLLKALEHSNSDVRGYAAFALGKIGS----ETAIGGLLKALEDSDEYVRRNAAFALGNIGS------ETAIQELLKA 233
Cdd:pfam01602  80 VTNSIQKDLQSPNQLIRGLALRTLSCIRVpelaRDLAPDIKKLLVDRSPYVRKKAALAILKLYRkspdlvRDFVPELKEL 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 234 LEDSDDwSVRRNAAFALAEIG-----TETAIPELLKALEDSNKDV----RIKAAEALGKIGSETA------ITGLLKALK 298
Cdd:pfam01602 160 LSDKDP-GVQSAAVALLYEICkndrlYLKLLPLLFRRLCNLLGVLnpwlQVKILRLLTRLAPLDPllpkelLEDLLNLLQ 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 299 DSNSIVRIKAAKALGNIGSET-----VIPGLLKALEDSDRYVRRDAAQALGKISSETAIAGLLKALK------DSYFSVR 367
Cdd:pfam01602 239 NSNNAVLYETANTIVHLAPAPelivlAVNALGRLLSSPDENLRYVALRNLNKIVMKEPKAVQHLDLIifclktDDDISIR 318

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733579917 368 WKAVEALGKIGSETAIPGLLKAL-----EDSNSILRWKAAEALGNIGS------ETAIPGLLKALEHSNSNVR 429
Cdd:pfam01602 319 LRALDLLYALVNESNVKEIVKELlkyvhEIADPDFKIELVRAIGRLAEkfptdaEWYLDVLLDLLSLAGSYVV 391
PDS5 cd19953
Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. ...
 258-377 8.40e-09

Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. Together with WapI and Scc3, it is involved in the release of the cohesin complex from chromosomes during S phase. The core of the cohesin complex consists of a coiled-coiled heterodimer of Smc1 and Smc30, together with Scc1 (also called kleisin). Pds5 interacts with Scc1 via a conserved patch on the surface of its heat repeats. Pds5 also promotes the acetylation of Smc3 that protects cohesin from releasing activity in G2 phase.


Pssm-ID: 410996 [Multi-domain]  Cd Length: 630  Bit Score: 58.69  E-value: 8.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 258 AIPELLKA--------LEDSNKDVRIKAAEALGKIGSETAITGL-----------LKALKDSNSIVRIKAAKALGNI--- 315
Cdd:cd19953   238 IAPELLLSvipqleeeLKADDVDVRLLATKLLGKMFAEKGSAGFaqtypslwkefLGRFNDKSPEVRLAWVESAKHIlln 317

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733579917 316 ---GSETVIPGLLKALEDSDRYVRRDAAQALGKISSETAIAG----LLKAL----KDSYFSVRWKAVEALGKI 377
Cdd:cd19953   318 hpdLAEDILEALKKRLLDPDEKVRLAAVKAICDLAYEDLLHKvpeeLLSTLaerlRDKKASVRKEALQGLARL 390
COG5096 COG5096
Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular ...
 164-260 2.07e-08

Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 227427 [Multi-domain]  Cd Length: 757  Bit Score: 57.82  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 164 AIAGLLKALEHSNSDVRGYAAFALGKIG----SETAIGGLLKALEDSDEYVRRNAAFALGNIGS-------ETAIQELLK 232
Cdd:COG5096    93 AVNTIQKDLQDPNEEIRGFALRTLSLLRvkelLGNIIDPIKKLLTDPHAYVRKTAALAVAKLYRldkdlyhELGLIDILK 172

                          90       100
                  ....*....|....*....|....*...
gi 1733579917 233 ALEDSDDWSVRRNAAFALAEIGTETAIP 260
Cdd:COG5096   173 ELVADSDPIVIANALASLAEIDPELAHG 200
PRK09687 PRK09687
putative lyase; Provisional
 143-400 5.18e-08

putative lyase; Provisional


Pssm-ID: 170047 [Multi-domain]  Cd Length: 280  Bit Score: 54.75  E-value: 5.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 143 DSNKDVREYAAYALGNISSETAIAGLLKALEHSNSDVRGYAAFALGKIGSETAIGGLLKALEDSDEYVRRNAAFALGNIG 222
Cdd:PRK09687    3 NSYKKRKASKEYSLYSQCKKLNDDELFRLLDDHNSLKRISSIRVLQLRGGQDVFRLAIELCSSKNPIERDIGADILSQLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 223 ----SETAIQELLKAL-EDSDDWSVRRNAAFALAEIGT-----ETAIPELLKALE-DSNKDVRIKAAEALGKIGSETAIT 291
Cdd:PRK09687   83 makrCQDNVFNILNNLaLEDKSACVRASAINATGHRCKknplySPKIVEQSQITAfDKSTNVRFAVAFALSVINDEAAIP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 292 GLLKALKDSNSIVRIKAAKALGN--IGSETVIPGLLKALEDSDRYVRRDAAQALGKISSETAIAGLLKALKDSyfSVRWK 369
Cdd:PRK09687  163 LLINLLKDPNGDVRNWAAFALNSnkYDNPDIREAFVAMLQDKNEEIRIEAIIGLALRKDKRVLSVLIKELKKG--TVGDL 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1733579917 370 AVEALGKIGSETAIPGL---LKALEDSNSILRWK 400
Cdd:PRK09687  241 IIEAAGELGDKTLLPVLdtlLYKFDDNEIITKAI 274
Adaptin_N pfam01602
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
 9-359 1.37e-07

Adaptin N terminal region; This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles.


Pssm-ID: 396262 [Multi-domain]  Cd Length: 523  Bit Score: 54.55  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917   9 AIAGLLKALEHSNSDVRGYAAFALGKIGS----ETAIGGLLKALEDSDEYVRRSAAFALGKIgsetaiggllkaLEDSDE 84
Cdd:pfam01602  80 VTNSIQKDLQSPNQLIRGLALRTLSCIRVpelaRDLAPDIKKLLVDRSPYVRKKAALAILKL------------YRKSPD 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  85 YVRMYAAKalgnigsetaitgLLKALEDSDEDVLWNAAEALgkigTEttiaglLKALEDSNKDVREYAAYALGNISSETA 164
Cdd:pfam01602 148 LVRDFVPE-------------LKELLSDKDPGVQSAAVALL----YE------ICKNDRLYLKLLPLLFRRLCNLLGVLN 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 165 ------IAGLLKALEHSNSDvrgyaafalgkiGSETAIGGLLKALEDSDEYVRRNAAFALGNIGSET-----AIQELLKA 233
Cdd:pfam01602 205 pwlqvkILRLLTRLAPLDPL------------LPKELLEDLLNLLQNSNNAVLYETANTIVHLAPAPelivlAVNALGRL 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 234 LEDSDDwSVRRNAAFALAEIGTETaiPELLKALE--------DSNKDVRIKAAEALGKIGSETAITGLLKALKD-----S 300
Cdd:pfam01602 273 LSSPDE-NLRYVALRNLNKIVMKE--PKAVQHLDliifclktDDDISIRLRALDLLYALVNESNVKEIVKELLKyvheiA 349

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1733579917 301 NSIVRIKAAKALGNIGS------ETVIPGLLKALEDSDRYVRRDAAQALGKI------SSETAIAGLLKAL 359
Cdd:pfam01602 350 DPDFKIELVRAIGRLAEkfptdaEWYLDVLLDLLSLAGSYVVDEIVEVIRDIiqnvpeLREYILEHLCELL 420
TIR smart00255
Toll - interleukin 1 - resistance;
493-608 2.08e-07

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 50.78  E-value: 2.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  493 QVYISYNWQEDS-NEMANQLVQAFDAKGIEI-IRDKTHtsYKDSIKNFMRQIGRGKCVVAVISDRYLKSENCMFELVEIA 570
Cdd:smart00255   3 DVFISYSGKEDVrNEFLSHLLEKLRGYGLCVfIDDFEP--GGGDLEEIDEAIEKSRIAIVVLSPNYAESEWCLDELVAAL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1733579917  571 RN--GDFYKRIFPIIL---------PDARIYKDFeRIDYLKYWEDEKAK 608
Cdd:smart00255  81 ENalEEGGLRVIPIFYevipsdvrkQPGKFRKVF-KKNYLKWPEDEKEQ 128
EZ_HEAT smart00567
E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other ...
 240-269 6.59e-07

E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other proteins. Probable scaffolding role.


Pssm-ID: 128837 [Multi-domain]  Cd Length: 30  Bit Score: 45.87  E-value: 6.59e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 1733579917  240 WSVRRNAAFALAEIGTETAIPELLKALEDS 269
Cdd:smart00567   1 PLVRHEAAFALGQLGDEEAVPALIKALEDE 30
EZ_HEAT smart00567
E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other ...
 208-237 6.99e-07

E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other proteins. Probable scaffolding role.


Pssm-ID: 128837 [Multi-domain]  Cd Length: 30  Bit Score: 45.87  E-value: 6.99e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 1733579917  208 EYVRRNAAFALGNIGSETAIQELLKALEDS 237
Cdd:smart00567   1 PLVRHEAAFALGQLGDEEAVPALIKALEDE 30
HEAT_EZ pfam13513
HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats ...
 240-284 1.56e-06

HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see pfam00514). These EZ repeats are found in subunits of cyanobacterial phycocyanin lyase and other proteins and probably carry out a scaffolding role.


Pssm-ID: 463906 [Multi-domain]  Cd Length: 55  Bit Score: 45.44  E-value: 1.56e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1733579917 240 WSVRRNAAFALAEIGTET----------AIPELLKALEDSNKDVRIKAAEALGKI 284
Cdd:pfam13513   1 WRVREAAALALGSLAEGGpdllapavpeLLPALLPLLNDDSDLVREAAAWALGRL 55
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 211-256 1.65e-06

Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; Epoxyqueuosine reductase QueG (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441208 [Multi-domain]  Cd Length: 345  Bit Score: 50.59  E-value: 1.65e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1733579917 211 RRNAAFALGNIGSETAIQELLKALEDSDDWsVRRNAAFALAEIGTE 256
Cdd:COG1600   300 LRNAAIALGNSGDPAAVPALEALLDDPSPL-VREHAAWALGRLGGR 344
PRK09687 PRK09687
putative lyase; Provisional
 2-147 1.88e-06

putative lyase; Provisional


Pssm-ID: 170047 [Multi-domain]  Cd Length: 280  Bit Score: 50.13  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917   2 GNISSETAIAGLLKALEHSNS-DVRGYAAFALGKIGSETAIGGLLKALEDSDEYVRRSAAFALG--KIGSETAIGGLLKA 78
Cdd:PRK09687  121 KNPLYSPKIVEQSQITAFDKStNVRFAVAFALSVINDEAAIPLLINLLKDPNGDVRNWAAFALNsnKYDNPDIREAFVAM 200

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1733579917  79 LEDSDEYVRMYAAKALGNIGSETAITGLLKALEDSDEDVLwnAAEALGKIGTETTIAGLLKALEDSNKD 147
Cdd:PRK09687  201 LQDKNEEIRIEAIIGLALRKDKRVLSVLIKELKKGTVGDL--IIEAAGELGDKTLLPVLDTLLYKFDDN 267
RPN2 COG5116
26S proteasome regulatory complex component [Posttranslational modification, protein turnover, ...
 198-408 4.35e-06

26S proteasome regulatory complex component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227446 [Multi-domain]  Cd Length: 926  Bit Score: 50.33  E-value: 4.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 198 GLLKA--LEDSDEYVRRN---------------AAFALGNIGSETAIQELLKALED---SDDWSVRRNAAFALAEIGTET 257
Cdd:COG5116   398 GLIKAgfGREDTEYLLEYfldtedeltpelaygVCLGIGLINMGSANREIYEKLKEllkNDRALLGEAAVYGMGLLMLGT 477

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 258 AIPELLKALEDSNKDV---RIKAAEALG----KIGSETAITGLLKAL-KDSNSIVRIKAAKALG----NIGSETVIPGLL 325
Cdd:COG5116   478 WSVEAIEDMRTYAGETqheRIKRGLGIGfaliLYGRQEMADDYINELlYDKDSILRYNGVFSLAlayvGTGNLGVVSTLL 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 326 K-ALEDSDRYVRRDAAQALGKI--SSETAIAGLLKALKDSY-FSVRWKAVEALG----KIGSETAIPGLLKALEDSNSIL 397
Cdd:COG5116   558 HyAVSDGNDDVRRAAVIALGFVccDDRDLLVGTVELLSESHnFHVRAGVAVALGiacaGTGDKVATDILEALMYDTNDFV 637

                         250
                  ....*....|.
gi 1733579917 398 RWKAAEALGNI 408
Cdd:COG5116   638 RQSAMIAVGMI 648
EZ_HEAT smart00567
E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other ...
 53-82 1.10e-05

E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other proteins. Probable scaffolding role.


Pssm-ID: 128837 [Multi-domain]  Cd Length: 30  Bit Score: 42.40  E-value: 1.10e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1733579917   53 EYVRRSAAFALGKIGSETAIGGLLKALEDS 82
Cdd:smart00567   1 PLVRHEAAFALGQLGDEEAVPALIKALEDE 30
EZ_HEAT smart00567
E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other ...
 365-393 1.20e-05

E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other proteins. Probable scaffolding role.


Pssm-ID: 128837 [Multi-domain]  Cd Length: 30  Bit Score: 42.40  E-value: 1.20e-05
                           10        20
                   ....*....|....*....|....*....
gi 1733579917  365 SVRWKAVEALGKIGSETAIPGLLKALEDS 393
Cdd:smart00567   2 LVRHEAAFALGQLGDEEAVPALIKALEDE 30
EZ_HEAT smart00567
E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other ...
 84-113 1.53e-05

E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other proteins. Probable scaffolding role.


Pssm-ID: 128837 [Multi-domain]  Cd Length: 30  Bit Score: 42.02  E-value: 1.53e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1733579917   84 EYVRMYAAKALGNIGSETAITGLLKALEDS 113
Cdd:smart00567   1 PLVRHEAAFALGQLGDEEAVPALIKALEDE 30
HEAT_PBS pfam03130
PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to ...
 242-268 2.79e-05

PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to pfam02985. Cyanobacteria and red algae harvest light energy using macromolecular complexes known as phycobilisomes (PBS), peripherally attached to the photosynthetic membrane. The major components of PBS are the phycobiliproteins. These heterodimeric proteins are covalently attached to phycobilins: open-chain tetrapyrrole chromophores, which function as the photosynthetic light-harvesting pigments. Phycobiliproteins differ in sequence and in the nature and number of attached phycobilins to each of their subunits. This family includes the lyase enzymes that specifically attach particular phycobilins to apophycobiliprotein subunits. The most comprehensively studied of these is the CpcE/F lyase, which attaches phycocyanobilin (PCB) to the alpha subunit of apophycocyanin. Similarly, MpeU/V attaches phycoerythrobilin to phycoerythrin II, while CpeY/Z is thought to be involved in phycoerythrobilin (PEB) attachment to phycoerythrin (PE) I (PEs I and II differ in sequence and in the number of attached molecules of PEB: PE I has five, PE II has six). All the reactions of the above lyases involve an apoprotein cysteine SH addition to a terminal delta 3,3'-double bond. Such a reaction is not possible in the case of phycoviolobilin (PVB), the phycobilin of alpha-phycoerythrocyanin (alpha-PEC). It is thought that in this case, PCB, not PVB, is first added to apo-alpha-PEC, and is then isomerized to PVB. The addition reaction has been shown to occur in the presence of either of the components of alpha-PEC-PVB lyase PecE or PecF (or both). The isomerization reaction occurs only when both PecE and PecF components are present, i.e. the PecE/F phycobiliprotein lyase is also a phycobilin isomerase. Another member of this family is the NblB protein, whose similarity to the phycobiliprotein lyases was previously noted. This constitutively expressed protein is not known to have any lyase activity. It is thought to be involved in the coordination of PBS degradation with environmental nutrient limitation. It has been suggested that the similarity of NblB to the phycobiliprotein lyases is due to the ability to bind tetrapyrrole phycobilins via the common repeated motif.


Pssm-ID: 308641 [Multi-domain]  Cd Length: 27  Bit Score: 41.31  E-value: 2.79e-05
                          10        20
                  ....*....|....*....|....*..
gi 1733579917 242 VRRNAAFALAEIGTETAIPELLKALED 268
Cdd:pfam03130   1 VRRAAARALGALGDPEAIPALIEALDD 27
Cnd1 pfam12717
non-SMC mitotic condensation complex subunit 1; The three non-SMC (structural maintenance of ...
 199-281 3.06e-05

non-SMC mitotic condensation complex subunit 1; The three non-SMC (structural maintenance of chromosomes) subunits of the mitotic condensation complex are Cnd1-3. The whole complex is essential for viability and the condensing of chromosomes in mitosis.


Pssm-ID: 463677 [Multi-domain]  Cd Length: 162  Bit Score: 44.76  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 199 LLKALEDSDEYVRRNAAFALGN------IGSETAIQELLKALEDSDDwSVRRNAAFALAEIGT--ETAI----PE----L 262
Cdd:pfam12717  26 LYRRLKDEDPYVRKTAAMCVAKlilpdmVKVKGFISELAKLLEDPNP-MVVANALAALTEISEkdPNAIynllPDiiskL 104

                          90
                  ....*....|....*....
gi 1733579917 263 LKALEDSNKDVRIKAAEAL 281
Cdd:pfam12717 105 SDALNECSEWGQIYILDFL 123
HEAT_PBS pfam03130
PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to ...
 210-236 3.32e-05

PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to pfam02985. Cyanobacteria and red algae harvest light energy using macromolecular complexes known as phycobilisomes (PBS), peripherally attached to the photosynthetic membrane. The major components of PBS are the phycobiliproteins. These heterodimeric proteins are covalently attached to phycobilins: open-chain tetrapyrrole chromophores, which function as the photosynthetic light-harvesting pigments. Phycobiliproteins differ in sequence and in the nature and number of attached phycobilins to each of their subunits. This family includes the lyase enzymes that specifically attach particular phycobilins to apophycobiliprotein subunits. The most comprehensively studied of these is the CpcE/F lyase, which attaches phycocyanobilin (PCB) to the alpha subunit of apophycocyanin. Similarly, MpeU/V attaches phycoerythrobilin to phycoerythrin II, while CpeY/Z is thought to be involved in phycoerythrobilin (PEB) attachment to phycoerythrin (PE) I (PEs I and II differ in sequence and in the number of attached molecules of PEB: PE I has five, PE II has six). All the reactions of the above lyases involve an apoprotein cysteine SH addition to a terminal delta 3,3'-double bond. Such a reaction is not possible in the case of phycoviolobilin (PVB), the phycobilin of alpha-phycoerythrocyanin (alpha-PEC). It is thought that in this case, PCB, not PVB, is first added to apo-alpha-PEC, and is then isomerized to PVB. The addition reaction has been shown to occur in the presence of either of the components of alpha-PEC-PVB lyase PecE or PecF (or both). The isomerization reaction occurs only when both PecE and PecF components are present, i.e. the PecE/F phycobiliprotein lyase is also a phycobilin isomerase. Another member of this family is the NblB protein, whose similarity to the phycobiliprotein lyases was previously noted. This constitutively expressed protein is not known to have any lyase activity. It is thought to be involved in the coordination of PBS degradation with environmental nutrient limitation. It has been suggested that the similarity of NblB to the phycobiliprotein lyases is due to the ability to bind tetrapyrrole phycobilins via the common repeated motif.


Pssm-ID: 308641 [Multi-domain]  Cd Length: 27  Bit Score: 40.93  E-value: 3.32e-05
                          10        20
                  ....*....|....*....|....*..
gi 1733579917 210 VRRNAAFALGNIGSETAIQELLKALED 236
Cdd:pfam03130   1 VRRAAARALGALGDPEAIPALIEALDD 27
EZ_HEAT smart00567
E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other ...
 397-424 3.42e-05

E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other proteins. Probable scaffolding role.


Pssm-ID: 128837 [Multi-domain]  Cd Length: 30  Bit Score: 41.25  E-value: 3.42e-05
                           10        20
                   ....*....|....*....|....*...
gi 1733579917  397 LRWKAAEALGNIGSETAIPGLLKALEHS 424
Cdd:smart00567   3 VRHEAAFALGQLGDEEAVPALIKALEDE 30
HEAT_EZ pfam13513
HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats ...
 148-190 4.27e-05

HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see pfam00514). These EZ repeats are found in subunits of cyanobacterial phycocyanin lyase and other proteins and probably carry out a scaffolding role.


Pssm-ID: 463906 [Multi-domain]  Cd Length: 55  Bit Score: 41.58  E-value: 4.27e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1733579917 148 VREYAAYALGNISSET----------AIAGLLKALEHSNSDVRGYAAFALGKI 190
Cdd:pfam13513   3 VREAAALALGSLAEGGpdllapavpeLLPALLPLLNDDSDLVREAAAWALGRL 55
COG5096 COG5096
Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular ...
 9-66 6.16e-05

Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 227427 [Multi-domain]  Cd Length: 757  Bit Score: 46.26  E-value: 6.16e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1733579917   9 AIAGLLKALEHSNSDVRGYAAFALGKIG----SETAIGGLLKALEDSDEYVRRSAAFALGKI 66
Cdd:COG5096    93 AVNTIQKDLQDPNEEIRGFALRTLSLLRvkelLGNIIDPIKKLLTDPHAYVRKTAALAVAKL 154
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 152-193 6.86e-05

Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; Epoxyqueuosine reductase QueG (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441208 [Multi-domain]  Cd Length: 345  Bit Score: 45.58  E-value: 6.86e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1733579917 152 AAYALGNISSETAIAGLLKALEHSNSDVRGYAAFALGKIGSE 193
Cdd:COG1600   303 AAIALGNSGDPAAVPALEALLDDPSPLVREHAAWALGRLGGR 344
Adaptin_N pfam01602
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
 289-487 7.98e-05

Adaptin N terminal region; This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles.


Pssm-ID: 396262 [Multi-domain]  Cd Length: 523  Bit Score: 45.69  E-value: 7.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 289 AITGLLKALKDSNSIVRIKAAKALGNIGS----ETVIPGLLKALEDSDRYVRRDAAQALGKI------SSETAIAGLLKA 358
Cdd:pfam01602  80 VTNSIQKDLQSPNQLIRGLALRTLSCIRVpelaRDLAPDIKKLLVDRSPYVRKKAALAILKLyrkspdLVRDFVPELKEL 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 359 LKDSYFSVRWKAVEALGKIG-----SETAIPGLLK----ALEDSNSILRWKAAEALGNIGSETA------IPGLLKALEH 423
Cdd:pfam01602 160 LSDKDPGVQSAAVALLYEICkndrlYLKLLPLLFRrlcnLLGVLNPWLQVKILRLLTRLAPLDPllpkelLEDLLNLLQN 239

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1733579917 424 SNSNVrVYAAV-ALGKIGTE-----AAMTELIKCLKNPD----FVTLNNGDTL----FQARKALDTIQNKLKYYHPLS 487
Cdd:pfam01602 240 SNNAV-LYETAnTIVHLAPApelivLAVNALGRLLSSPDenlrYVALRNLNKIvmkePKAVQHLDLIIFCLKTDDDIS 316
EZ_HEAT smart00567
E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other ...
 304-331 1.06e-04

E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other proteins. Probable scaffolding role.


Pssm-ID: 128837 [Multi-domain]  Cd Length: 30  Bit Score: 39.71  E-value: 1.06e-04
                           10        20
                   ....*....|....*....|....*...
gi 1733579917  304 VRIKAAKALGNIGSETVIPGLLKALEDS 331
Cdd:smart00567   3 VRHEAAFALGQLGDEEAVPALIKALEDE 30
EZ_HEAT smart00567
E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other ...
 24-51 1.11e-04

E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other proteins. Probable scaffolding role.


Pssm-ID: 128837 [Multi-domain]  Cd Length: 30  Bit Score: 39.71  E-value: 1.11e-04
                           10        20
                   ....*....|....*....|....*...
gi 1733579917   24 VRGYAAFALGKIGSETAIGGLLKALEDS 51
Cdd:smart00567   3 VRHEAAFALGQLGDEEAVPALIKALEDE 30
EZ_HEAT smart00567
E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other ...
 179-206 1.11e-04

E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other proteins. Probable scaffolding role.


Pssm-ID: 128837 [Multi-domain]  Cd Length: 30  Bit Score: 39.71  E-value: 1.11e-04
                           10        20
                   ....*....|....*....|....*...
gi 1733579917  179 VRGYAAFALGKIGSETAIGGLLKALEDS 206
Cdd:smart00567   3 VRHEAAFALGQLGDEEAVPALIKALEDE 30
EZ_HEAT smart00567
E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other ...
 273-300 2.39e-04

E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other proteins. Probable scaffolding role.


Pssm-ID: 128837 [Multi-domain]  Cd Length: 30  Bit Score: 38.55  E-value: 2.39e-04
                           10        20
                   ....*....|....*....|....*...
gi 1733579917  273 VRIKAAEALGKIGSETAITGLLKALKDS 300
Cdd:smart00567   3 VRHEAAFALGQLGDEEAVPALIKALEDE 30
HEAT_EZ pfam13513
HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats ...
 54-97 2.58e-04

HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see pfam00514). These EZ repeats are found in subunits of cyanobacterial phycocyanin lyase and other proteins and probably carry out a scaffolding role.


Pssm-ID: 463906 [Multi-domain]  Cd Length: 55  Bit Score: 39.27  E-value: 2.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1733579917  54 YVRRSAAFALGKIGSET----------AIGGLLKALEDSDEYVRMYAAKALGNI 97
Cdd:pfam13513   2 RVREAAALALGSLAEGGpdllapavpeLLPALLPLLNDDSDLVREAAAWALGRL 55
HEAT_PBS pfam03130
PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to ...
 366-392 2.77e-04

PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to pfam02985. Cyanobacteria and red algae harvest light energy using macromolecular complexes known as phycobilisomes (PBS), peripherally attached to the photosynthetic membrane. The major components of PBS are the phycobiliproteins. These heterodimeric proteins are covalently attached to phycobilins: open-chain tetrapyrrole chromophores, which function as the photosynthetic light-harvesting pigments. Phycobiliproteins differ in sequence and in the nature and number of attached phycobilins to each of their subunits. This family includes the lyase enzymes that specifically attach particular phycobilins to apophycobiliprotein subunits. The most comprehensively studied of these is the CpcE/F lyase, which attaches phycocyanobilin (PCB) to the alpha subunit of apophycocyanin. Similarly, MpeU/V attaches phycoerythrobilin to phycoerythrin II, while CpeY/Z is thought to be involved in phycoerythrobilin (PEB) attachment to phycoerythrin (PE) I (PEs I and II differ in sequence and in the number of attached molecules of PEB: PE I has five, PE II has six). All the reactions of the above lyases involve an apoprotein cysteine SH addition to a terminal delta 3,3'-double bond. Such a reaction is not possible in the case of phycoviolobilin (PVB), the phycobilin of alpha-phycoerythrocyanin (alpha-PEC). It is thought that in this case, PCB, not PVB, is first added to apo-alpha-PEC, and is then isomerized to PVB. The addition reaction has been shown to occur in the presence of either of the components of alpha-PEC-PVB lyase PecE or PecF (or both). The isomerization reaction occurs only when both PecE and PecF components are present, i.e. the PecE/F phycobiliprotein lyase is also a phycobilin isomerase. Another member of this family is the NblB protein, whose similarity to the phycobiliprotein lyases was previously noted. This constitutively expressed protein is not known to have any lyase activity. It is thought to be involved in the coordination of PBS degradation with environmental nutrient limitation. It has been suggested that the similarity of NblB to the phycobiliprotein lyases is due to the ability to bind tetrapyrrole phycobilins via the common repeated motif.


Pssm-ID: 308641 [Multi-domain]  Cd Length: 27  Bit Score: 38.61  E-value: 2.77e-04
                          10        20
                  ....*....|....*....|....*..
gi 1733579917 366 VRWKAVEALGKIGSETAIPGLLKALED 392
Cdd:pfam03130   1 VRRAAARALGALGDPEAIPALIEALDD 27
HEAT_PBS pfam03130
PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to ...
 86-112 5.61e-04

PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to pfam02985. Cyanobacteria and red algae harvest light energy using macromolecular complexes known as phycobilisomes (PBS), peripherally attached to the photosynthetic membrane. The major components of PBS are the phycobiliproteins. These heterodimeric proteins are covalently attached to phycobilins: open-chain tetrapyrrole chromophores, which function as the photosynthetic light-harvesting pigments. Phycobiliproteins differ in sequence and in the nature and number of attached phycobilins to each of their subunits. This family includes the lyase enzymes that specifically attach particular phycobilins to apophycobiliprotein subunits. The most comprehensively studied of these is the CpcE/F lyase, which attaches phycocyanobilin (PCB) to the alpha subunit of apophycocyanin. Similarly, MpeU/V attaches phycoerythrobilin to phycoerythrin II, while CpeY/Z is thought to be involved in phycoerythrobilin (PEB) attachment to phycoerythrin (PE) I (PEs I and II differ in sequence and in the number of attached molecules of PEB: PE I has five, PE II has six). All the reactions of the above lyases involve an apoprotein cysteine SH addition to a terminal delta 3,3'-double bond. Such a reaction is not possible in the case of phycoviolobilin (PVB), the phycobilin of alpha-phycoerythrocyanin (alpha-PEC). It is thought that in this case, PCB, not PVB, is first added to apo-alpha-PEC, and is then isomerized to PVB. The addition reaction has been shown to occur in the presence of either of the components of alpha-PEC-PVB lyase PecE or PecF (or both). The isomerization reaction occurs only when both PecE and PecF components are present, i.e. the PecE/F phycobiliprotein lyase is also a phycobilin isomerase. Another member of this family is the NblB protein, whose similarity to the phycobiliprotein lyases was previously noted. This constitutively expressed protein is not known to have any lyase activity. It is thought to be involved in the coordination of PBS degradation with environmental nutrient limitation. It has been suggested that the similarity of NblB to the phycobiliprotein lyases is due to the ability to bind tetrapyrrole phycobilins via the common repeated motif.


Pssm-ID: 308641 [Multi-domain]  Cd Length: 27  Bit Score: 37.46  E-value: 5.61e-04
                          10        20
                  ....*....|....*....|....*..
gi 1733579917  86 VRMYAAKALGNIGSETAITGLLKALED 112
Cdd:pfam03130   1 VRRAAARALGALGDPEAIPALIEALDD 27
EZ_HEAT smart00567
E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other ...
 334-362 5.79e-04

E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other proteins. Probable scaffolding role.


Pssm-ID: 128837 [Multi-domain]  Cd Length: 30  Bit Score: 37.78  E-value: 5.79e-04
                           10        20
                   ....*....|....*....|....*....
gi 1733579917  334 YVRRDAAQALGKISSETAIAGLLKALKDS 362
Cdd:smart00567   2 LVRHEAAFALGQLGDEEAVPALIKALEDE 30
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 120-162 5.93e-04

Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; Epoxyqueuosine reductase QueG (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441208 [Multi-domain]  Cd Length: 345  Bit Score: 42.50  E-value: 5.93e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1733579917 120 NAAEALGKIGTETTIAGLLKALEDSNKDVREYAAYALGNISSE 162
Cdd:COG1600   302 NAAIALGNSGDPAAVPALEALLDDPSPLVREHAAWALGRLGGR 344
EZ_HEAT smart00567
E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other ...
 148-175 6.64e-04

E-Z type HEAT repeats; Present in subunits of cyanobacterial phycocyanin lyase, and other proteins. Probable scaffolding role.


Pssm-ID: 128837 [Multi-domain]  Cd Length: 30  Bit Score: 37.40  E-value: 6.64e-04
                           10        20
                   ....*....|....*....|....*...
gi 1733579917  148 VREYAAYALGNISSETAIAGLLKALEHS 175
Cdd:smart00567   3 VRHEAAFALGQLGDEEAVPALIKALEDE 30
PRK09687 PRK09687
putative lyase; Provisional
 297-437 6.97e-04

putative lyase; Provisional


Pssm-ID: 170047 [Multi-domain]  Cd Length: 280  Bit Score: 42.04  E-value: 6.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 297 LKDSNSIVRIKAAKALGNIGSETVIPGLLKALEDSDRYVRRDAAQALGKIS----SETAIAGLLKAL--KDSYFSVRWKA 370
Cdd:PRK09687   32 LDDHNSLKRISSIRVLQLRGGQDVFRLAIELCSSKNPIERDIGADILSQLGmakrCQDNVFNILNNLalEDKSACVRASA 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733579917 371 VEALG------KIGSETAIPGLLKALEDSNSILRWKAAEALGNIGSETAIPGLLKALEHSNSNVRVYAAVALG 437
Cdd:PRK09687  112 INATGhrckknPLYSPKIVEQSQITAFDKSTNVRFAVAFALSVINDEAAIPLLINLLKDPNGDVRNWAAFALN 184
HEAT_PBS pfam03130
PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to ...
 397-423 7.45e-04

PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to pfam02985. Cyanobacteria and red algae harvest light energy using macromolecular complexes known as phycobilisomes (PBS), peripherally attached to the photosynthetic membrane. The major components of PBS are the phycobiliproteins. These heterodimeric proteins are covalently attached to phycobilins: open-chain tetrapyrrole chromophores, which function as the photosynthetic light-harvesting pigments. Phycobiliproteins differ in sequence and in the nature and number of attached phycobilins to each of their subunits. This family includes the lyase enzymes that specifically attach particular phycobilins to apophycobiliprotein subunits. The most comprehensively studied of these is the CpcE/F lyase, which attaches phycocyanobilin (PCB) to the alpha subunit of apophycocyanin. Similarly, MpeU/V attaches phycoerythrobilin to phycoerythrin II, while CpeY/Z is thought to be involved in phycoerythrobilin (PEB) attachment to phycoerythrin (PE) I (PEs I and II differ in sequence and in the number of attached molecules of PEB: PE I has five, PE II has six). All the reactions of the above lyases involve an apoprotein cysteine SH addition to a terminal delta 3,3'-double bond. Such a reaction is not possible in the case of phycoviolobilin (PVB), the phycobilin of alpha-phycoerythrocyanin (alpha-PEC). It is thought that in this case, PCB, not PVB, is first added to apo-alpha-PEC, and is then isomerized to PVB. The addition reaction has been shown to occur in the presence of either of the components of alpha-PEC-PVB lyase PecE or PecF (or both). The isomerization reaction occurs only when both PecE and PecF components are present, i.e. the PecE/F phycobiliprotein lyase is also a phycobilin isomerase. Another member of this family is the NblB protein, whose similarity to the phycobiliprotein lyases was previously noted. This constitutively expressed protein is not known to have any lyase activity. It is thought to be involved in the coordination of PBS degradation with environmental nutrient limitation. It has been suggested that the similarity of NblB to the phycobiliprotein lyases is due to the ability to bind tetrapyrrole phycobilins via the common repeated motif.


Pssm-ID: 308641 [Multi-domain]  Cd Length: 27  Bit Score: 37.46  E-value: 7.45e-04
                          10        20
                  ....*....|....*....|....*..
gi 1733579917 397 LRWKAAEALGNIGSETAIPGLLKALEH 423
Cdd:pfam03130   1 VRRAAARALGALGDPEAIPALIEALDD 27
COG5096 COG5096
Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular ...
 289-346 7.80e-04

Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 227427 [Multi-domain]  Cd Length: 757  Bit Score: 42.79  E-value: 7.80e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1733579917 289 AITGLLKALKDSNSIVRIKAAKALGNIG----SETVIPGLLKALEDSDRYVRRDAAQALGKI 346
Cdd:COG5096    93 AVNTIQKDLQDPNEEIRGFALRTLSLLRvkelLGNIIDPIKKLLTDPHAYVRKTAALAVAKL 154
HEAT_PBS pfam03130
PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to ...
 304-330 9.81e-04

PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to pfam02985. Cyanobacteria and red algae harvest light energy using macromolecular complexes known as phycobilisomes (PBS), peripherally attached to the photosynthetic membrane. The major components of PBS are the phycobiliproteins. These heterodimeric proteins are covalently attached to phycobilins: open-chain tetrapyrrole chromophores, which function as the photosynthetic light-harvesting pigments. Phycobiliproteins differ in sequence and in the nature and number of attached phycobilins to each of their subunits. This family includes the lyase enzymes that specifically attach particular phycobilins to apophycobiliprotein subunits. The most comprehensively studied of these is the CpcE/F lyase, which attaches phycocyanobilin (PCB) to the alpha subunit of apophycocyanin. Similarly, MpeU/V attaches phycoerythrobilin to phycoerythrin II, while CpeY/Z is thought to be involved in phycoerythrobilin (PEB) attachment to phycoerythrin (PE) I (PEs I and II differ in sequence and in the number of attached molecules of PEB: PE I has five, PE II has six). All the reactions of the above lyases involve an apoprotein cysteine SH addition to a terminal delta 3,3'-double bond. Such a reaction is not possible in the case of phycoviolobilin (PVB), the phycobilin of alpha-phycoerythrocyanin (alpha-PEC). It is thought that in this case, PCB, not PVB, is first added to apo-alpha-PEC, and is then isomerized to PVB. The addition reaction has been shown to occur in the presence of either of the components of alpha-PEC-PVB lyase PecE or PecF (or both). The isomerization reaction occurs only when both PecE and PecF components are present, i.e. the PecE/F phycobiliprotein lyase is also a phycobilin isomerase. Another member of this family is the NblB protein, whose similarity to the phycobiliprotein lyases was previously noted. This constitutively expressed protein is not known to have any lyase activity. It is thought to be involved in the coordination of PBS degradation with environmental nutrient limitation. It has been suggested that the similarity of NblB to the phycobiliprotein lyases is due to the ability to bind tetrapyrrole phycobilins via the common repeated motif.


Pssm-ID: 308641 [Multi-domain]  Cd Length: 27  Bit Score: 37.07  E-value: 9.81e-04
                          10        20
                  ....*....|....*....|....*..
gi 1733579917 304 VRIKAAKALGNIGSETVIPGLLKALED 330
Cdd:pfam03130   1 VRRAAARALGALGDPEAIPALIEALDD 27
HEAT_PBS pfam03130
PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to ...
 55-81 1.15e-03

PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to pfam02985. Cyanobacteria and red algae harvest light energy using macromolecular complexes known as phycobilisomes (PBS), peripherally attached to the photosynthetic membrane. The major components of PBS are the phycobiliproteins. These heterodimeric proteins are covalently attached to phycobilins: open-chain tetrapyrrole chromophores, which function as the photosynthetic light-harvesting pigments. Phycobiliproteins differ in sequence and in the nature and number of attached phycobilins to each of their subunits. This family includes the lyase enzymes that specifically attach particular phycobilins to apophycobiliprotein subunits. The most comprehensively studied of these is the CpcE/F lyase, which attaches phycocyanobilin (PCB) to the alpha subunit of apophycocyanin. Similarly, MpeU/V attaches phycoerythrobilin to phycoerythrin II, while CpeY/Z is thought to be involved in phycoerythrobilin (PEB) attachment to phycoerythrin (PE) I (PEs I and II differ in sequence and in the number of attached molecules of PEB: PE I has five, PE II has six). All the reactions of the above lyases involve an apoprotein cysteine SH addition to a terminal delta 3,3'-double bond. Such a reaction is not possible in the case of phycoviolobilin (PVB), the phycobilin of alpha-phycoerythrocyanin (alpha-PEC). It is thought that in this case, PCB, not PVB, is first added to apo-alpha-PEC, and is then isomerized to PVB. The addition reaction has been shown to occur in the presence of either of the components of alpha-PEC-PVB lyase PecE or PecF (or both). The isomerization reaction occurs only when both PecE and PecF components are present, i.e. the PecE/F phycobiliprotein lyase is also a phycobilin isomerase. Another member of this family is the NblB protein, whose similarity to the phycobiliprotein lyases was previously noted. This constitutively expressed protein is not known to have any lyase activity. It is thought to be involved in the coordination of PBS degradation with environmental nutrient limitation. It has been suggested that the similarity of NblB to the phycobiliprotein lyases is due to the ability to bind tetrapyrrole phycobilins via the common repeated motif.


Pssm-ID: 308641 [Multi-domain]  Cd Length: 27  Bit Score: 36.69  E-value: 1.15e-03
                          10        20
                  ....*....|....*....|....*..
gi 1733579917  55 VRRSAAFALGKIGSETAIGGLLKALED 81
Cdd:pfam03130   1 VRRAAARALGALGDPEAIPALIEALDD 27
HEAT_EZ pfam13513
HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats ...
 209-253 1.21e-03

HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see pfam00514). These EZ repeats are found in subunits of cyanobacterial phycocyanin lyase and other proteins and probably carry out a scaffolding role.


Pssm-ID: 463906 [Multi-domain]  Cd Length: 55  Bit Score: 37.35  E-value: 1.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1733579917 209 YVRRNAAFALGNIGSET----------AIQELLKALEDSDDwSVRRNAAFALAEI 253
Cdd:pfam13513   2 RVREAAALALGSLAEGGpdllapavpeLLPALLPLLNDDSD-LVREAAAWALGRL 55
HEAT_PBS pfam03130
PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to ...
 273-299 1.59e-03

PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to pfam02985. Cyanobacteria and red algae harvest light energy using macromolecular complexes known as phycobilisomes (PBS), peripherally attached to the photosynthetic membrane. The major components of PBS are the phycobiliproteins. These heterodimeric proteins are covalently attached to phycobilins: open-chain tetrapyrrole chromophores, which function as the photosynthetic light-harvesting pigments. Phycobiliproteins differ in sequence and in the nature and number of attached phycobilins to each of their subunits. This family includes the lyase enzymes that specifically attach particular phycobilins to apophycobiliprotein subunits. The most comprehensively studied of these is the CpcE/F lyase, which attaches phycocyanobilin (PCB) to the alpha subunit of apophycocyanin. Similarly, MpeU/V attaches phycoerythrobilin to phycoerythrin II, while CpeY/Z is thought to be involved in phycoerythrobilin (PEB) attachment to phycoerythrin (PE) I (PEs I and II differ in sequence and in the number of attached molecules of PEB: PE I has five, PE II has six). All the reactions of the above lyases involve an apoprotein cysteine SH addition to a terminal delta 3,3'-double bond. Such a reaction is not possible in the case of phycoviolobilin (PVB), the phycobilin of alpha-phycoerythrocyanin (alpha-PEC). It is thought that in this case, PCB, not PVB, is first added to apo-alpha-PEC, and is then isomerized to PVB. The addition reaction has been shown to occur in the presence of either of the components of alpha-PEC-PVB lyase PecE or PecF (or both). The isomerization reaction occurs only when both PecE and PecF components are present, i.e. the PecE/F phycobiliprotein lyase is also a phycobilin isomerase. Another member of this family is the NblB protein, whose similarity to the phycobiliprotein lyases was previously noted. This constitutively expressed protein is not known to have any lyase activity. It is thought to be involved in the coordination of PBS degradation with environmental nutrient limitation. It has been suggested that the similarity of NblB to the phycobiliprotein lyases is due to the ability to bind tetrapyrrole phycobilins via the common repeated motif.


Pssm-ID: 308641 [Multi-domain]  Cd Length: 27  Bit Score: 36.30  E-value: 1.59e-03
                          10        20
                  ....*....|....*....|....*..
gi 1733579917 273 VRIKAAEALGKIGSETAITGLLKALKD 299
Cdd:pfam03130   1 VRRAAARALGALGDPEAIPALIEALDD 27
HEAT pfam02985
HEAT repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see ...
 259-286 1.90e-03

HEAT repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see pfam00514).


Pssm-ID: 460773  Cd Length: 31  Bit Score: 36.35  E-value: 1.90e-03
                          10        20
                  ....*....|....*....|....*...
gi 1733579917 259 IPELLKALEDSNKDVRIKAAEALGKIGS 286
Cdd:pfam02985   2 LPLLLKLLNDPSPEVREAAAEALGELAE 29
COG5096 COG5096
Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular ...
 40-125 2.18e-03

Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 227427 [Multi-domain]  Cd Length: 757  Bit Score: 41.25  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  40 AIGGLLKALEDSDEYVRRSAAFALGKIG----SETAIGGLLKALEDSDEYVRMYAAKALGNI--------GSETAITGLL 107
Cdd:COG5096    93 AVNTIQKDLQDPNEEIRGFALRTLSLLRvkelLGNIIDPIKKLLTDPHAYVRKTAALAVAKLyrldkdlyHELGLIDILK 172

                          90
                  ....*....|....*...
gi 1733579917 108 KALEDSDEDVLWNAAEAL 125
Cdd:COG5096   173 ELVADSDPIVIANALASL 190
HEAT_EZ pfam13513
HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats ...
 365-408 2.91e-03

HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see pfam00514). These EZ repeats are found in subunits of cyanobacterial phycocyanin lyase and other proteins and probably carry out a scaffolding role.


Pssm-ID: 463906 [Multi-domain]  Cd Length: 55  Bit Score: 36.58  E-value: 2.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1733579917 365 SVRWKAVEALGKIGSET----------AIPGLLKALEDSNSILRWKAAEALGNI 408
Cdd:pfam13513   2 RVREAAALALGSLAEGGpdllapavpeLLPALLPLLNDDSDLVREAAAWALGRL 55
HEAT_EZ pfam13513
HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats ...
 179-221 3.15e-03

HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see pfam00514). These EZ repeats are found in subunits of cyanobacterial phycocyanin lyase and other proteins and probably carry out a scaffolding role.


Pssm-ID: 463906 [Multi-domain]  Cd Length: 55  Bit Score: 36.19  E-value: 3.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1733579917 179 VRGYAAFALGKIGSET----------AIGGLLKALEDSDEYVRRNAAFALGNI 221
Cdd:pfam13513   3 VREAAALALGSLAEGGpdllapavpeLLPALLPLLNDDSDLVREAAAWALGRL 55
COG5096 COG5096
Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular ...
 382-439 3.25e-03

Vesicle coat complex, various subunits [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 227427 [Multi-domain]  Cd Length: 757  Bit Score: 40.87  E-value: 3.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1733579917 382 AIPGLLKALEDSNSILRWKAAEALGNIG----SETAIPGLLKALEHSNSNVRVYAAVALGKI 439
Cdd:COG5096    93 AVNTIQKDLQDPNEEIRGFALRTLSLLRvkelLGNIIDPIKKLLTDPHAYVRKTAALAVAKL 154
HEAT_EZ pfam13513
HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats ...
 117-159 3.76e-03

HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see pfam00514). These EZ repeats are found in subunits of cyanobacterial phycocyanin lyase and other proteins and probably carry out a scaffolding role.


Pssm-ID: 463906 [Multi-domain]  Cd Length: 55  Bit Score: 36.19  E-value: 3.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1733579917 117 VLWNAAEALGKIGTETT----------IAGLLKALEDSNKDVREYAAYALGNI 159
Cdd:pfam13513   3 VREAAALALGSLAEGGPdllapavpelLPALLPLLNDDSDLVREAAAWALGRL 55
HEAT_PBS pfam03130
PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to ...
 179-205 3.84e-03

PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to pfam02985. Cyanobacteria and red algae harvest light energy using macromolecular complexes known as phycobilisomes (PBS), peripherally attached to the photosynthetic membrane. The major components of PBS are the phycobiliproteins. These heterodimeric proteins are covalently attached to phycobilins: open-chain tetrapyrrole chromophores, which function as the photosynthetic light-harvesting pigments. Phycobiliproteins differ in sequence and in the nature and number of attached phycobilins to each of their subunits. This family includes the lyase enzymes that specifically attach particular phycobilins to apophycobiliprotein subunits. The most comprehensively studied of these is the CpcE/F lyase, which attaches phycocyanobilin (PCB) to the alpha subunit of apophycocyanin. Similarly, MpeU/V attaches phycoerythrobilin to phycoerythrin II, while CpeY/Z is thought to be involved in phycoerythrobilin (PEB) attachment to phycoerythrin (PE) I (PEs I and II differ in sequence and in the number of attached molecules of PEB: PE I has five, PE II has six). All the reactions of the above lyases involve an apoprotein cysteine SH addition to a terminal delta 3,3'-double bond. Such a reaction is not possible in the case of phycoviolobilin (PVB), the phycobilin of alpha-phycoerythrocyanin (alpha-PEC). It is thought that in this case, PCB, not PVB, is first added to apo-alpha-PEC, and is then isomerized to PVB. The addition reaction has been shown to occur in the presence of either of the components of alpha-PEC-PVB lyase PecE or PecF (or both). The isomerization reaction occurs only when both PecE and PecF components are present, i.e. the PecE/F phycobiliprotein lyase is also a phycobilin isomerase. Another member of this family is the NblB protein, whose similarity to the phycobiliprotein lyases was previously noted. This constitutively expressed protein is not known to have any lyase activity. It is thought to be involved in the coordination of PBS degradation with environmental nutrient limitation. It has been suggested that the similarity of NblB to the phycobiliprotein lyases is due to the ability to bind tetrapyrrole phycobilins via the common repeated motif.


Pssm-ID: 308641 [Multi-domain]  Cd Length: 27  Bit Score: 35.15  E-value: 3.84e-03
                          10        20
                  ....*....|....*....|....*..
gi 1733579917 179 VRGYAAFALGKIGSETAIGGLLKALED 205
Cdd:pfam03130   1 VRRAAARALGALGDPEAIPALIEALDD 27
HEAT_PBS pfam03130
PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to ...
 24-50 3.84e-03

PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to pfam02985. Cyanobacteria and red algae harvest light energy using macromolecular complexes known as phycobilisomes (PBS), peripherally attached to the photosynthetic membrane. The major components of PBS are the phycobiliproteins. These heterodimeric proteins are covalently attached to phycobilins: open-chain tetrapyrrole chromophores, which function as the photosynthetic light-harvesting pigments. Phycobiliproteins differ in sequence and in the nature and number of attached phycobilins to each of their subunits. This family includes the lyase enzymes that specifically attach particular phycobilins to apophycobiliprotein subunits. The most comprehensively studied of these is the CpcE/F lyase, which attaches phycocyanobilin (PCB) to the alpha subunit of apophycocyanin. Similarly, MpeU/V attaches phycoerythrobilin to phycoerythrin II, while CpeY/Z is thought to be involved in phycoerythrobilin (PEB) attachment to phycoerythrin (PE) I (PEs I and II differ in sequence and in the number of attached molecules of PEB: PE I has five, PE II has six). All the reactions of the above lyases involve an apoprotein cysteine SH addition to a terminal delta 3,3'-double bond. Such a reaction is not possible in the case of phycoviolobilin (PVB), the phycobilin of alpha-phycoerythrocyanin (alpha-PEC). It is thought that in this case, PCB, not PVB, is first added to apo-alpha-PEC, and is then isomerized to PVB. The addition reaction has been shown to occur in the presence of either of the components of alpha-PEC-PVB lyase PecE or PecF (or both). The isomerization reaction occurs only when both PecE and PecF components are present, i.e. the PecE/F phycobiliprotein lyase is also a phycobilin isomerase. Another member of this family is the NblB protein, whose similarity to the phycobiliprotein lyases was previously noted. This constitutively expressed protein is not known to have any lyase activity. It is thought to be involved in the coordination of PBS degradation with environmental nutrient limitation. It has been suggested that the similarity of NblB to the phycobiliprotein lyases is due to the ability to bind tetrapyrrole phycobilins via the common repeated motif.


Pssm-ID: 308641 [Multi-domain]  Cd Length: 27  Bit Score: 35.15  E-value: 3.84e-03
                          10        20
                  ....*....|....*....|....*..
gi 1733579917  24 VRGYAAFALGKIGSETAIGGLLKALED 50
Cdd:pfam03130   1 VRRAAARALGALGDPEAIPALIEALDD 27
Adaptin_N pfam01602
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
 195-454 3.94e-03

Adaptin N terminal region; This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles.


Pssm-ID: 396262 [Multi-domain]  Cd Length: 523  Bit Score: 40.30  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 195 AIGGLLKALEDSDEYVRRNAAFALGNIGS----ETAIQELLKALEDSDDwSVRRNAAFALAEI------GTETAIPELLK 264
Cdd:pfam01602  80 VTNSIQKDLQSPNQLIRGLALRTLSCIRVpelaRDLAPDIKKLLVDRSP-YVRKKAALAILKLyrkspdLVRDFVPELKE 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 265 ALEDSNKDVRIKAAEALGKIGSE---------TAITGLLKALKDSNSIVRIKAAKALGNIG------SETVIPGLLKALE 329
Cdd:pfam01602 159 LLSDKDPGVQSAAVALLYEICKNdrlylkllpLLFRRLCNLLGVLNPWLQVKILRLLTRLApldpllPKELLEDLLNLLQ 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 330 DSDRYVRRDAAQALGKISSET-----AIAGLLKALKDSYFSVRWKAVEALGKIGSETaiPGLLKALE--------DSNSI 396
Cdd:pfam01602 239 NSNNAVLYETANTIVHLAPAPelivlAVNALGRLLSSPDENLRYVALRNLNKIVMKE--PKAVQHLDliifclktDDDIS 316

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1733579917 397 LRWKAAEALGNIGSETAIPGLLKAL-----EHSNSNVRVYAAVALG----KIGTEAA--MTELIKCLKN 454
Cdd:pfam01602 317 IRLRALDLLYALVNESNVKEIVKELlkyvhEIADPDFKIELVRAIGrlaeKFPTDAEwyLDVLLDLLSL 385
SEC21 COG5240
Vesicle coat complex COPI, gamma subunit [Intracellular trafficking and secretion];
208-460 4.25e-03

Vesicle coat complex COPI, gamma subunit [Intracellular trafficking and secretion];


Pssm-ID: 227565 [Multi-domain]  Cd Length: 898  Bit Score: 40.37  E-value: 4.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 208 EYVRRNAAFALGNIGSE--TAIQELLKALEDSDDWSVRRNAAFALAEIG------TETAIPELLKALEDSNKDVRIKAAE 279
Cdd:COG5240   283 EAARAVCALSEENVGSQfvDQTVSSLRTFLKSTRVVLRFSAMRILNQLAmkypqkVSVCNKEVESLISDENRTISTYAIT 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 280 ALGKIGSETAITGLLKA-------LKDSNSIVRIKAAKALGNI---GSETVIPGLLKALEDSDRY-VRRDAAQALGKI-- 346
Cdd:COG5240   363 TLLKTGTEETIDRLVNLipsfvhdMSDGFKIIAIDALRSLSLLfpsKKLSYLDFLGSSLLQEGGLeFKKYMVDAISDAme 442

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 347 ----SSETAIAGLLKALKDS-YFSVRWKAVEALGKIGSETAIPGL-----LKALEDSNSILRWKAAEALGNIG------- 409
Cdd:COG5240   443 ndpdSKERALEVLCTFIEDCeYHQITVRILGILGREGPRAKTPGKyvrhiYNRLILENNIVRSAAVQALSKFAlnisdvv 522

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1733579917 410 -SETAIPGLLKALEHSNSNVRVYAAVALGKIGTEAAMTELIKCLKNPDFVTL 460
Cdd:COG5240   523 sPQSVENALKRCLNDQDDEVRDRASFLLRNMRLSDACEPLFSSDELGDIPSL 574
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 40-267 4.30e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 39.71  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  40 AIGGLLKALEDSDEYVRrsAAFALGKIGS-----ETAIGGLLKALEDSDE--YVRMYAAKALGNIGS-ETAITGLLKALE 111
Cdd:COG2956    27 AIDLLEEALELDPETVE--AHLALGNLYRrrgeyDRAIRIHQKLLERDPDraEALLELAQDYLKAGLlDRAEELLEKLLE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 112 DSDEDVlwNAAEALGKIGTET-----TIAGLLKALEDSNKDVR---EYAAYALGNISSETAIAGLLKALEHSNSDVRgyA 183
Cdd:COG2956   105 LDPDDA--EALRLLAEIYEQEgdwekAIEVLERLLKLGPENAHaycELAELYLEQGDYDEAIEALEKALKLDPDCAR--A 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 184 AFALGKIGSET-----AIGGLLKALEDSDEYVR-----RNAAFALGNIgsETAIQELLKALEDSDDWSVRRNAAFALAEI 253
Cdd:COG2956   181 LLLLAELYLEQgdyeeAIAALERALEQDPDYLPalprlAELYEKLGDP--EEALELLRKALELDPSDDLLLALADLLERK 258

                         250
                  ....*....|....*
gi 1733579917 254 -GTETAIPELLKALE 267
Cdd:COG2956   259 eGLEAALALLERQLR 273
HEAT_EZ pfam13513
HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats ...
 397-439 4.41e-03

HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see pfam00514). These EZ repeats are found in subunits of cyanobacterial phycocyanin lyase and other proteins and probably carry out a scaffolding role.


Pssm-ID: 463906 [Multi-domain]  Cd Length: 55  Bit Score: 35.81  E-value: 4.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1733579917 397 LRWKAAEALGNIGSET----------AIPGLLKALEHSNSNVRVYAAVALGKI 439
Cdd:pfam13513   3 VREAAALALGSLAEGGpdllapavpeLLPALLPLLNDDSDLVREAAAWALGRL 55
HEAT_PBS pfam03130
PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to ...
 148-174 4.59e-03

PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to pfam02985. Cyanobacteria and red algae harvest light energy using macromolecular complexes known as phycobilisomes (PBS), peripherally attached to the photosynthetic membrane. The major components of PBS are the phycobiliproteins. These heterodimeric proteins are covalently attached to phycobilins: open-chain tetrapyrrole chromophores, which function as the photosynthetic light-harvesting pigments. Phycobiliproteins differ in sequence and in the nature and number of attached phycobilins to each of their subunits. This family includes the lyase enzymes that specifically attach particular phycobilins to apophycobiliprotein subunits. The most comprehensively studied of these is the CpcE/F lyase, which attaches phycocyanobilin (PCB) to the alpha subunit of apophycocyanin. Similarly, MpeU/V attaches phycoerythrobilin to phycoerythrin II, while CpeY/Z is thought to be involved in phycoerythrobilin (PEB) attachment to phycoerythrin (PE) I (PEs I and II differ in sequence and in the number of attached molecules of PEB: PE I has five, PE II has six). All the reactions of the above lyases involve an apoprotein cysteine SH addition to a terminal delta 3,3'-double bond. Such a reaction is not possible in the case of phycoviolobilin (PVB), the phycobilin of alpha-phycoerythrocyanin (alpha-PEC). It is thought that in this case, PCB, not PVB, is first added to apo-alpha-PEC, and is then isomerized to PVB. The addition reaction has been shown to occur in the presence of either of the components of alpha-PEC-PVB lyase PecE or PecF (or both). The isomerization reaction occurs only when both PecE and PecF components are present, i.e. the PecE/F phycobiliprotein lyase is also a phycobilin isomerase. Another member of this family is the NblB protein, whose similarity to the phycobiliprotein lyases was previously noted. This constitutively expressed protein is not known to have any lyase activity. It is thought to be involved in the coordination of PBS degradation with environmental nutrient limitation. It has been suggested that the similarity of NblB to the phycobiliprotein lyases is due to the ability to bind tetrapyrrole phycobilins via the common repeated motif.


Pssm-ID: 308641 [Multi-domain]  Cd Length: 27  Bit Score: 35.15  E-value: 4.59e-03
                          10        20
                  ....*....|....*....|....*..
gi 1733579917 148 VREYAAYALGNISSETAIAGLLKALEH 174
Cdd:pfam03130   1 VRRAAARALGALGDPEAIPALIEALDD 27
RPN2 COG5116
26S proteasome regulatory complex component [Posttranslational modification, protein turnover, ...
 3-157 5.38e-03

26S proteasome regulatory complex component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227446 [Multi-domain]  Cd Length: 926  Bit Score: 40.32  E-value: 5.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917   3 NISSETAIAGLLKALEHS-NSDVRGYAAFALGK----IGSETAIGGLLK-ALEDSDEYVRRSAAFALGKI--GSETAIGG 74
Cdd:COG5116   510 LYGRQEMADDYINELLYDkDSILRYNGVFSLALayvgTGNLGVVSTLLHyAVSDGNDDVRRAAVIALGFVccDDRDLLVG 589

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917  75 LLKALEDS-DEYVRMYAAKALG----NIGSETAITGLLKALEDSDEDVLWNAAEALGKIGTETT------IAGLLKALED 143
Cdd:COG5116   590 TVELLSEShNFHVRAGVAVALGiacaGTGDKVATDILEALMYDTNDFVRQSAMIAVGMILMQCNpelnpnVKRIIKKFNR 669

                         170
                  ....*....|....
gi 1733579917 144 SNKDVREYAAYALG 157
Cdd:COG5116   670 VIVDKHESGLAKLG 683
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 1-38 6.01e-03

Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; Epoxyqueuosine reductase QueG (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441208 [Multi-domain]  Cd Length: 345  Bit Score: 39.42  E-value: 6.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1733579917   1 MGNISSETAIAGLLKALEHSNSDVRGYAAFALGKIGSE 38
Cdd:COG1600   307 LGNSGDPAAVPALEALLDDPSPLVREHAAWALGRLGGR 344
Vitellogenin_N pfam01347
Lipoprotein amino terminal region; This family contains regions from: Vitellogenin, Microsomal ...
 159-346 6.07e-03

Lipoprotein amino terminal region; This family contains regions from: Vitellogenin, Microsomal triglyceride transfer protein and apolipoprotein B-100. These proteins are all involved in lipid transport. This family contains the LV1n chain from lipovitellin, that contains two structural domains.


Pssm-ID: 460170 [Multi-domain]  Cd Length: 582  Bit Score: 39.95  E-value: 6.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 159 ISSETAIAGLLKALEHSNSDVRGYAAF--ALGKIGSETAigglLKALED--SDEYVRRN-AAFALGNIGS-ETAIQELLK 232
Cdd:pfam01347 330 TASEEQLEQIWRQLYQNKPKYRRWPAFldAVAQAGTGPA----LKFIKQwiKSKKITGLeAAQVLAVLPHaRYPTEEYMK 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733579917 233 ALED--SDDWS-----VRRNAAFALAEigtetaipeLLKALEDSNKDVRIKAAEALGKIGSEtaitgLLKALKDSNSIVR 305
Cdd:pfam01347 406 ALFElaESPEVknqpyLNTSALLAYGS---------LVRKYCVNNPSCPREFEEYLPPLAQK-----LKEAVSKGDSEKI 471

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1733579917 306 IKAAKALGNIGSETVIPGLLKALEDSDR---YVRRDAAQALGKI 346
Cdd:pfam01347 472 QLYLKALGNAGHPESLKVLEKYLEGAEGlstRVRVAAVQALRNL 515
HEAT_EZ pfam13513
HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats ...
 304-346 6.60e-03

HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see pfam00514). These EZ repeats are found in subunits of cyanobacterial phycocyanin lyase and other proteins and probably carry out a scaffolding role.


Pssm-ID: 463906 [Multi-domain]  Cd Length: 55  Bit Score: 35.42  E-value: 6.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1733579917 304 VRIKAAKALGNIGSET----------VIPGLLKALEDSDRYVRRDAAQALGKI 346
Cdd:pfam13513   3 VREAAALALGSLAEGGpdllapavpeLLPALLPLLNDDSDLVREAAAWALGRL 55
HEAT_PBS pfam03130
PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to ...
 335-361 7.21e-03

PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to pfam02985. Cyanobacteria and red algae harvest light energy using macromolecular complexes known as phycobilisomes (PBS), peripherally attached to the photosynthetic membrane. The major components of PBS are the phycobiliproteins. These heterodimeric proteins are covalently attached to phycobilins: open-chain tetrapyrrole chromophores, which function as the photosynthetic light-harvesting pigments. Phycobiliproteins differ in sequence and in the nature and number of attached phycobilins to each of their subunits. This family includes the lyase enzymes that specifically attach particular phycobilins to apophycobiliprotein subunits. The most comprehensively studied of these is the CpcE/F lyase, which attaches phycocyanobilin (PCB) to the alpha subunit of apophycocyanin. Similarly, MpeU/V attaches phycoerythrobilin to phycoerythrin II, while CpeY/Z is thought to be involved in phycoerythrobilin (PEB) attachment to phycoerythrin (PE) I (PEs I and II differ in sequence and in the number of attached molecules of PEB: PE I has five, PE II has six). All the reactions of the above lyases involve an apoprotein cysteine SH addition to a terminal delta 3,3'-double bond. Such a reaction is not possible in the case of phycoviolobilin (PVB), the phycobilin of alpha-phycoerythrocyanin (alpha-PEC). It is thought that in this case, PCB, not PVB, is first added to apo-alpha-PEC, and is then isomerized to PVB. The addition reaction has been shown to occur in the presence of either of the components of alpha-PEC-PVB lyase PecE or PecF (or both). The isomerization reaction occurs only when both PecE and PecF components are present, i.e. the PecE/F phycobiliprotein lyase is also a phycobilin isomerase. Another member of this family is the NblB protein, whose similarity to the phycobiliprotein lyases was previously noted. This constitutively expressed protein is not known to have any lyase activity. It is thought to be involved in the coordination of PBS degradation with environmental nutrient limitation. It has been suggested that the similarity of NblB to the phycobiliprotein lyases is due to the ability to bind tetrapyrrole phycobilins via the common repeated motif.


Pssm-ID: 308641 [Multi-domain]  Cd Length: 27  Bit Score: 34.38  E-value: 7.21e-03
                          10        20
                  ....*....|....*....|....*..
gi 1733579917 335 VRRDAAQALGKISSETAIAGLLKALKD 361
Cdd:pfam03130   1 VRRAAARALGALGDPEAIPALIEALDD 27
HEAT_PBS pfam03130
PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to ...
 428-454 8.78e-03

PBS lyase HEAT-like repeat; This family contains a short bi-helical repeat that is related to pfam02985. Cyanobacteria and red algae harvest light energy using macromolecular complexes known as phycobilisomes (PBS), peripherally attached to the photosynthetic membrane. The major components of PBS are the phycobiliproteins. These heterodimeric proteins are covalently attached to phycobilins: open-chain tetrapyrrole chromophores, which function as the photosynthetic light-harvesting pigments. Phycobiliproteins differ in sequence and in the nature and number of attached phycobilins to each of their subunits. This family includes the lyase enzymes that specifically attach particular phycobilins to apophycobiliprotein subunits. The most comprehensively studied of these is the CpcE/F lyase, which attaches phycocyanobilin (PCB) to the alpha subunit of apophycocyanin. Similarly, MpeU/V attaches phycoerythrobilin to phycoerythrin II, while CpeY/Z is thought to be involved in phycoerythrobilin (PEB) attachment to phycoerythrin (PE) I (PEs I and II differ in sequence and in the number of attached molecules of PEB: PE I has five, PE II has six). All the reactions of the above lyases involve an apoprotein cysteine SH addition to a terminal delta 3,3'-double bond. Such a reaction is not possible in the case of phycoviolobilin (PVB), the phycobilin of alpha-phycoerythrocyanin (alpha-PEC). It is thought that in this case, PCB, not PVB, is first added to apo-alpha-PEC, and is then isomerized to PVB. The addition reaction has been shown to occur in the presence of either of the components of alpha-PEC-PVB lyase PecE or PecF (or both). The isomerization reaction occurs only when both PecE and PecF components are present, i.e. the PecE/F phycobiliprotein lyase is also a phycobilin isomerase. Another member of this family is the NblB protein, whose similarity to the phycobiliprotein lyases was previously noted. This constitutively expressed protein is not known to have any lyase activity. It is thought to be involved in the coordination of PBS degradation with environmental nutrient limitation. It has been suggested that the similarity of NblB to the phycobiliprotein lyases is due to the ability to bind tetrapyrrole phycobilins via the common repeated motif.


Pssm-ID: 308641 [Multi-domain]  Cd Length: 27  Bit Score: 34.38  E-value: 8.78e-03
                          10        20
                  ....*....|....*....|....*..
gi 1733579917 428 VRVYAAVALGKIGTEAAMTELIKCLKN 454
Cdd:pfam03130   1 VRRAAARALGALGDPEAIPALIEALDD 27
HEAT_EZ pfam13513
HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats ...
 85-128 9.05e-03

HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see pfam00514). These EZ repeats are found in subunits of cyanobacterial phycocyanin lyase and other proteins and probably carry out a scaffolding role.


Pssm-ID: 463906 [Multi-domain]  Cd Length: 55  Bit Score: 35.04  E-value: 9.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1733579917  85 YVRMYAAKALGNIGSET----------AITGLLKALEDSDEDVLWNAAEALGKI 128
Cdd:pfam13513   2 RVREAAALALGSLAEGGpdllapavpeLLPALLPLLNDDSDLVREAAAWALGRL 55
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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